Top

Journal of Nanoparticle Research

Published in:

01-11-2022 | Review

Applications of mannose-binding lectins and mannan glycoconjugates in nanomedicine

Authors: Anita Gupta, G. S. Gupta

Published in: Journal of Nanoparticle Research | Issue 11/2022

Activate our intelligent search to find suitable subject content or patents.

search-config

AI-assisted search

Off

Abstract

Glycosylated nanoparticles (NPs) have drawn a lot of attention in the biomedical field over the past few decades, particularly in applications like targeted drug delivery. Mannosylated NPs and mannan-binding lectins/proteins (MBL/MBP) are emerging as promising tools for delivery of drugs, medicines, and enzymes to targeted tissues and cells as nanocarriers, enhancing their therapeutic benefits while avoiding the adverse effects of the drug. The occurrence of plenty of lectin receptors and their mannan ligands on cell surfaces makes them multifaceted carriers appropriate for specific delivery of bioactive drug materials to their targeted sites. Thus, the present review describes the tethering of mannose (Man) to several nanostructures, like micelles, liposomes, and other NPs, applicable for drug delivery systems. Bioadhesion through MBL-like receptors on cells has involvements applicable to additional arenas of science, for example gene delivery, tissue engineering, biomaterials, and nanotechnology. This review also focuses on the role of various aspects of drug/antigen delivery using (i) mannosylated NPs, (ii) mannosylated lectins, (iii) amphiphilic glycopolymer NPs, and (iv) natural mannan-containing polysaccharides, with most significant applications of MBL-based NPs as multivalent scaffolds, using different strategies.

Graphical abstract

Mannosylated NPs and/or MBL/MBP are coming up as viable and versatile tools as nanocarriers to deliver drugs and enzymes precisely to their target tissues or cells. The presence of abundant number of lectin receptors and their mannan ligands on cell surfaces makes them versatile carriers suitable for the targeted delivery of bioactive drugs.

next article Hierarchical phase separation in all small-molecule organic solar cells

Dont have a licence yet? Then find out more about our products and how to get one now:

Springer Professional "Wirtschaft+Technik"

Online-Abonnement

Mit Springer Professional "Wirtschaft+Technik" erhalten Sie Zugriff auf:

über 102.000 Bücher
über 537 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Finance + Banking
Management + Führung
Marketing + Vertrieb
Maschinenbau + Werkstoffe
Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

inform now

Springer Professional "Technik"

Online-Abonnement

Mit Springer Professional "Technik" erhalten Sie Zugriff auf:

über 67.000 Bücher
über 390 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Maschinenbau + Werkstoffe

Jetzt Wissensvorsprung sichern!

inform now

Tsaneva M, Van Damme EJM (2020) 130 years of plant lectin research. Glycoconj J 37:533–551. https://doi.org/10.1007/s10719-020-09942-yCrossRef

Gupta A, Sandhu RS (1997) A new high molecular weight agglutinin from garlic (Allium sativum). Mol Cell Biochem 166:1–9. https://doi.org/10.1023/a:1006827921151CrossRef

Gupta GS (2012) Animal lectins: form, function and clinical applications. Springer-Wien

Nizet V, Varki A, Aebi M (2017) Microbial lectins: hemagglutinins, adhesins, and toxins. In: A Varki, RD Cummings, JD Esko, (Eds) Essentials of glycobiology. 3rd ed. Cold Spring Harbor (NY), Ch 37.

Peumans WJ, Damme V (1995) EJM. Lectins as plant defence proteins. Plant Physiol 109:347–352. https://doi.org/10.1104/pp.109.2.347CrossRef

Gupta A (2020) Emerging applications of lectins in cancer detection and biomedicine. Mater Today: Proc 31:651–661. https://doi.org/10.1016/j.matpr.2020.05.810CrossRef

Muramoto K (2017) Lectins as bioactive proteins in foods and feeds. Food Sci Technol Res 23:487–494. https://doi.org/10.3136/fstr.23.487CrossRef

Gupta A, Sandhu RS (1998) Effect of garlic agglutinin and garlic extracts on the rat jejunum. Nutr Res 18:841–850. https://doi.org/10.1016/s0271-5317(98)00069-4CrossRef

Gupta A, Sandhu RS (1997) In vivo binding of mannose specific lectin from garlic to intestinal epithelium. Nutr Res 17:703–711. https://doi.org/10.1016/S0271-5317(97)00040-7CrossRef

10.

von Itzstein M (2008) Disease-associated carbohydrate-recognising proteins and structure-based inhibitor design. Curr Opin Struct Biol 18:558–566. https://doi.org/10.1016/j.sbi.2008.07.006CrossRef

11.

Lagarda-Diaz I, Guzman-Partida AM, Vazquez-Moreno L (2017) Legume lectins: proteins with diverse applications. Int J Mol Sci 18:1242–1260. https://doi.org/10.3390/ijms18061242CrossRef

12.

Katoch R, Tripathi A (2021) Research advances and prospects of legume lectins. J Biosci 46(4):104. https://doi.org/10.1007/s12038-021-00225-8CrossRef

13.

Dias Rde O, Machado Ldos S et al (2015) Insights into animal and plant lectins with antimicrobial activities. Molecules 20:519–541. https://doi.org/10.3390/molecules20010519CrossRef

14.

Cedzyński M, Świerzko AS (2020) Components of the lectin pathway of complement in haematologic malignancies. Cancers 12:1792–1810. https://doi.org/10.3390/cancers12071792CrossRef

15.

Sampaolesi S, Nicotra F, Russo L (2019) Glycans in nanomedicine, impact and perspectives. Future Med Chem 11:43–60. https://doi.org/10.4155/fmc-2018-0368CrossRef

16.

Hatton NE, Baumann CG, Fascione MA (2021) Developments in mannose-based treatments for uropathogenic Escherichia coli-induced urinary tract infections. ChemBioChem 22:613–629. https://doi.org/10.1002/cbic.202000406CrossRef

17.

Ofek I, Beachey EH (1978) Mannose binding and epithelial cell adherence of Escherichia coli. Infect Immun 22:247–254. https://doi.org/10.1128/iai.22.1.247-254.1978CrossRef

18.

Ohlsen K, Oelschlaeger TA, Hacker J et al (2009) Carbohydrate receptors of bacterial adhesion: implications and reflections. Top Curr Chem 288:109–120. https://doi.org/10.1007/128_2008_10CrossRef

19.

Hynes SO, Hirmo S, Wadstrom T et al (1999) Differentiation of Helicobacter pylori isolates based on lectin binding of cell extracts in an agglutination assay. J Clin Microbiol 37:1994–1998. https://doi.org/10.1128/JCM.37.6.1994-1998.1999CrossRef

20.

Botos I, Wlodawer A (2005) Proteins that bind high-mannose sugars of the HIV envelope. Prog Biophys Mol Biol 88:233–282. https://doi.org/10.1016/j.pbiomolbio.2004.05.001CrossRef

21.

Tchesnokova V, Aprikian P, Kisiela D et al (2011) Type 1 fimbrial adhesin FimH elicits an immune response that enhances cell adhesion of Escherichia coli. Infect Immun 79:3895–3904. https://doi.org/10.1128/IAI.05169-11CrossRef

22.

Cuenot S, Bouvrée A, Bouchara JP (2017) Nanoscale mapping of multiple lectins on cell surfaces by single-molecule force spectroscopy. Adv Biosys 1:1700050. https://doi.org/10.1002/adbi.201700050CrossRef

23.

Gupta A, Gupta RK, Gupta GS (2009) Targeting cells for drug and gene delivery: emerging applications of mannans and mannan binding lectins. J Sci Indus Res 68:465–483

24.

Barre A, Bourne Y, Van Damme EJM et al (2001) Mannose-binding plant lectins: different structural scaffolds for a common sugar-recognition process. Biochimie 83:645–651. https://doi.org/10.1016/s0300-9084(01)01315-3CrossRef

25.

Barre A, Simplicien M, Benoist H et al (2019) Mannose-specific lectins from marine algae: diverse structural scaffolds associated to common virucidal and anti-cancer properties. Mar Drugs 17:440. https://doi.org/10.3390/md17080440CrossRef

26.

Hwang HJ, Han JW, Jeon H et al (2020) Characterization of a novel mannose-lectin with antiviral activities from red alga Grateloupia chiangii. Biomolecules 10:333. https://doi.org/10.3390/biom10020333CrossRef

27.

Nabi-Afjadi M, Heydari M, Zalpoor H et al (2022) Lectins and lectibodies: potential promising antiviral agents. Cell Mol Biol Lett 27:37. https://doi.org/10.1186/s11658-022-00338-4CrossRef

28.

Martinez D, Amaral D, Markovitz D et al (2021) The use of lectins as tools to combat SARS-CoV-2. Curr Pharm Des 27(41):4212–4222. https://doi.org/10.2174/1381612827666210830094743CrossRef

29.

Gupta A (2012) Collectins: mannan-binding protein as a model lectin. In: Gupta GS (ed) Animal lectins: form, function and clinical applications. Springer-Wien, pp 483–499

30.

Stravalaci M, De Blasio D, Orsini V et al (2016) A new surface plasmon resonance assay for in vitro screening of mannose-binding lectin inhibitors. Biomol Screen 21:749–757. https://doi.org/10.1177/1087057116637563CrossRef

31.

Dørflinger GH, Holt CB, Thiel S et al (2017) Effect of optimization of glycaemic control on mannan-binding lectin in type 1 Diabetes. J Diabetes Res 2017:1249729. https://doi.org/10.1155/2017/1249729CrossRef

32.

De Blasio D, Fumagalli S, Longhi L et al (2017) Pharmacological inhibition of mannose-binding lectin ameliorates neurobehavioral dysfunction following experimental traumatic brain injury. J Cereb Blood Flow Metab 37:938–950. https://doi.org/10.1177/0271678X16647397CrossRef

33.

Meier M, Bider MD, Malashkevich VN et al (2000) Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor. J Mol Biol 300:857–865. https://doi.org/10.1006/jmbi.2000.3853CrossRef

34.

Wu J, Nantz MH, Zern MA (2002) Targeting hepatocytes for drug and gene delivery: emerging novel approaches and applications. Front Biosci 7:d717-725. https://doi.org/10.2741/A806CrossRef

35.

Hu J, Wei P, Seeberger PH, Yin J (2018) Mannose-functionalized nanoscaffolds for targeted delivery in biomedical applications. Chem Asian J 13:3448–3459. https://doi.org/10.1002/asia.201801088CrossRef

36.

Ip WK, Chan KH, Law HK et al (2005) Mannose-binding lectin in severe acute respiratory syndrome coronavirus infection. J Infect Dis 191:1697–1704. https://doi.org/10.1086/429631CrossRef

37.

Świerzko AS, Cedzyński M (2020) The influence of the lectin pathway of complement activation on infections of the respiratory system. Front Immunol 11:585243. https://doi.org/10.3389/fimmu.2020.585243CrossRef

38.

Medetalibeyoglu A, Bahat G, Senkal N et al (2021) Mannose binding lectin gene 2 (rs1800450) missense variant may contribute to development and severity of COVID-19 infection. Infect Genet Evol 89:104717. https://doi.org/10.1016/j.meegid.2021.104717CrossRef

39.

Gupta A, Gupta GS (2021) Status of mannose-binding lectin (MBL) and complement system in COVID-19 patients and therapeutic applications of antiviral plant MBLs. Mol Cell Biochem 21:1–26. https://doi.org/10.1007/s11010-021-04107-3CrossRef

40.

Ambrosio AR, De Messias-Reason IJ (2005) Leishmania (Viannia) braziliensis: interaction of mannose-binding lectin with surface glycoconjugates and complement activation An antibody-independent defence mechanism. Parasite Immunol 27:333–340. https://doi.org/10.1111/j.1365-3024.2005.00782.xCrossRef

41.

Zhang JX, Gong WP, Zhu DL et al (2020) Mannose-binding lectin 2 gene polymorphisms and their association with tuberculosis in a Chinese population. Infect Dis Poverty 9:46. https://doi.org/10.1186/s40249-020-00664-9CrossRef

42.

Ramos-Soriano J, Reina JJ, Illescas BM et al (2019) Synthesis of highly efficient multivalent disaccharide/[60] fullerene nanoballs for emergent viruses. J Am Chem Soc 141:15403–15412. https://doi.org/10.1021/jacs.9b08003CrossRef

43.

Bhute VJ, Harte J, Houghton JW et al (2020) Mannose binding lectin is hydroxylated by collagen prolyl-4-hydroxylase and inhibited by some PHD inhibitors. KIDNEY360. 1:447–457. https://doi.org/10.34067/KID.0000092020

44.

Gupta RK, Gupta GS (2012) Mannose receptor family: R-type lectins. In: Gupta GS (ed) Animal lectins: form, function and clinical applications. Springer-Wien, pp 331–347

45.

Boskovic J, Arnold JN, Stilion R et al (2006) Structural model for the mannose receptor family uncovered by electron microscopy of Endo180 and the mannose receptor. J Biol Chem 28:8780–8787. https://doi.org/10.1074/jbc.M513277200CrossRef

46.

Gupta RK, Gupta GS (2012) Dectin-1 receptor family. In: Gupta GS (ed) Animal lectins: form, function and clinical applications. Springer-Wien, pp 725–747

47.

Gupta RK, Gupta GS (2012) Dendritic cell lectin receptors (dectin-2 receptors family). In: Gupta GS (ed) Animal lectins: form, function and clinical applications, Springer-Wien, pp 749–771

48.

Huang X, Jain PK, El-Sayed IH et al (2007) Gold NPs: interesting optical properties and recent applications in cancer diagnostics and therapy. Nanomedicine 2:681–693. https://doi.org/10.2217/17435889.2.5.681CrossRef

49.

Napper CE, Dyson MH, Taylor ME (2001) An extended conformation of the macrophage mannose receptor. J Biol Chem 276:14759–14766. https://doi.org/10.1074/jbc.M100425200CrossRef

50.

Sedaghat B, Stephenson R, Toth I (2014) Targeting the mannose receptor with mannosylated subunit vaccines. Curr Med Chem 21:3405–3418. https://doi.org/10.2174/0929867321666140826115552CrossRef

51.

Feinberg H, Mitchell DA, Drickamer K et al (2001) Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 294:2163–2166. https://doi.org/10.1126/science.1066371CrossRef

52.

Gupta RK, Gupta GS (2012) DC-SIGN family of receptors. In: Gupta GS (ed) Animal lectins: form, function and clinical applications. Springer-Wien, pp 773–798

53.

Gupta RK, Gupta A (2012) Endogenous lectins as drug targets. In: Gupta GS (ed) Animal lectins: form, function and clinical applications. Springer-Wien, pp 1039–1057

54.

Dennehy KM, Brown GD (2007) The role of the β-glucan receptor dectin-1 in control of fungal infection. J Leuko Biol 82:253–258. https://doi.org/10.1189/jlb.1206753CrossRef

55.

Blattes E, Vercellone A, Eutamène H et al (2013) Mannodendrimers prevent acute lung inflammation by inhibiting neutrophil recruitment. Proc Natl Acad Sci USA 110:8795–8800. https://doi.org/10.1073/pnas.1221708110CrossRef

56.

Engleder E, Demmerer E, Wang X et al (2015) Determination of the glycosylation-pattern of the middle ear mucosa in guinea pigs. Int J Pharm 484:124–130. https://doi.org/10.1016/j.ijpharm.2015.02.056CrossRef

57.

Gonzalez SF, Kornek VL, Kuligowski MP et al (2010) Capture of influenza by medullary dendritic cells via SIGN-R1 is essential for humoral immunity in draining lymph nodes. Nat Immunol 11:427–434. https://doi.org/10.1038/ni.1856CrossRef

58.

Tzeng CW, Tzeng WS, Lin LT et al (2016) Enhanced autophagic activity of artocarpin in human hepatocellular carcinoma cells through improving its solubility by a NP system. Phytomedicine 23:528–540. https://doi.org/10.1016/j.phymed.2016.02.010CrossRef

59.

Kwankaew J, Phimnuan P, Wanauppathamkul S et al (2017) Formulation of chitosan patch incorporating Artocarpus altilis heartwood extract for improving hyperpigmentation. J Cosmet Sci 68:257–269

60.

Omokawa Y, Miyazaki T, Walde P, Akiyama K, Sugahara T et al (2010) In vitro and in vivo anti-tumor effects of novel Span 80 vesicles containing immobilized Eucheuma serra agglutinin. Int J Pharm 389:157–167. https://doi.org/10.1016/j.ijpharm.2010.01.033CrossRef

61.

Condori J, Acosta W, Ayala J et al (2016) Enzyme replacement for GM1-gangliosidosis: uptake, lysosomal activation, and cellular disease correction using a novel β-galactosidase: RTB lectin fusion. Mol Genet Metab 117:199–209. https://doi.org/10.1016/j.ymgme.2015.12.002CrossRef

62.

Acosta W, Ayala J, Dolan MC et al (2015) RTB Lectin: a novel receptor-independent delivery system for lysosomal enzyme replacement therapies. Sci Rep 5:14144. https://doi.org/10.1038/srep14144CrossRef

63.

Bitsch M, Laursen I, Engel AM et al (2009) Epidemiology of chronic wound patients and relation to serum levels of mannan-binding lectin. Acta Derm Venereol 89:607–611. https://doi.org/10.2340/00015555-0730CrossRef

64.

Maaløe CB, Laursen I et al (2011) Mannan-binding lectin and healing of a radiation-induced chronic ulcer—a case report on mannan-binding lectin replacement therapy. Plast Reconstr Aesthet 64:e146–e148. https://doi.org/10.1016/j.bjps.2011.01.013CrossRef

65.

Chahud F, Ramalho LNZ, Ramalho FS et al (2009) The lectin KM+ induces corneal epithelial wound healing in rabbits. Int J Exp Pathol 90:166–173. https://doi.org/10.1111/j.1365-2613.2008.00626.xCrossRef

66.

Van EJ, Van Baardewijk LJ, Sier CF et al (2013) Bone healing and mannose-binding lectin. Int J Surg 11:296–300. https://doi.org/10.1016/j.ijsu.2013.02.022CrossRef

67.

Axelgaard E, Østergaard JA, Thiel S et al (2017) Diabetes is associated with increased autoreactivity of mannan-binding lectin. J Diabetes Res 2017:6368780. https://doi.org/10.1155/2017/6368780CrossRef

68.

Demir EF, Atay NO, Koruyucu M et al (2018) Mannose based polymeric nanoparticles for lectin separation. Sep Sci Technol 53:1–11. https://doi.org/10.1080/01496395.2018.1452943CrossRef

69.

Tetala KKR, Chen B, Visser GM et al (2007) Preparation of a monolithic capillary column with immobilized α-mannose for affinity chromatography of lectins. J Biochem Biophys Methods 70:63–69. https://doi.org/10.1016/j.jbbm.2006.09.009CrossRef

70.

Bamrungsap S, Zhao Z, Chen T et al (2012) A focus on NPs as a drug delivery system. Nanomedicine 7:1253–1271. https://doi.org/10.2217/nnm.12.87CrossRef

71.

Sinha R, Kim GJ, Nie S et al (2006) Nanotechnology in cancer therapeutics: bioconjugated NPs for drug delivery. Mol Cancer Ther 5:1909–1917. https://doi.org/10.1158/1535-7163.MCT-06-0141CrossRef

72.

Yilmaz G, Becer CR (2015) Glyconanoparticles and their interactions with lectins. Polym Chem 6:5503–5514. https://doi.org/10.1039/c5py00089kCrossRef

73.

Cho K, Wang X, Nie S et al (2008) Therapeutic NPs for drug delivery in cancer. Clin Cancer Res 14:1310–1316. https://doi.org/10.1158/1078-0432.CCR-07-1441CrossRef

74.

Sahoo SK, Labhasetwar V (2005) Enhanced antiproliferative activity of transferrin-conjugated paclitaxel-loaded NPs is mediated via sustained intracellular drug retention. Mol Pharm 2:373–383. https://doi.org/10.1021/mp050032zCrossRef

75.

Smith AM, Duan H, Mohs AM et al (2008) Bioconjugated quantum dots for in vivo molecular and cellular imaging. Adv Drug Deliv Rev 60:1226–1240. https://doi.org/10.1016/j.addr.2008.03.015CrossRef

76.

Kubik T, Bogunia K, Sugisaka M (2005) Nanotechnology on duty in medical applications. Curr Pharm Biotechnol 6:17–33. https://doi.org/10.2174/1389201053167248CrossRef

77.

Yatvin MB, Kreut W, Horwitz BA et al (1980) pH-sensitive liposomes: possible clinical implications. Science 10:1253–1255. https://doi.org/10.1126/science.7434025CrossRef

78.

Salata O (2004) Applications of nanoparticles in biology and medicine. J Nanobiotechnol 2:3. https://doi.org/10.1186/1477-3155-2-3CrossRef

79.

Khan I, Khalid S, Idrees K (2019) Nanoparticles: properties, applications and toxicities. Arab J Chem 12:908–931. https://doi.org/10.1016/j.arabjc.2017.05.011CrossRef

80.

Cha C, Shin SR, Annabi N et al (2013) Carbon-based nanomaterials: multi-functional materials for biomedical engineering. ACS Nano 7:2891–2897. https://doi.org/10.1021/nn401196aCrossRef

81.

Andersen AJ, Robinson JT, Dai H et al (2013) Single-walled carbon nanotube surface control of complement recognition and activation. ACS Nano 7:1108–1119. https://doi.org/10.1021/nn3055175CrossRef

82.

Fard MG, Khabir Z, Reineck P et al (2022) Targeting cell surface glycans with lectin-coated fluorescent nanodiamonds. Nanoscale Adv 4:1551–1564. https://doi.org/10.1039/d2na00036aCrossRef

83.

Tripathi SK, Kaur G, Khurana RK, Kapoor S, Singh B (2015) Quantum dots and their potential role in cancer theranostics. Crit Rev Ther Drug Carr Sys 32:461–502. https://doi.org/10.1615/critrevtherdrugcarriersyst.2015012360CrossRef

84.

Toraskar S, Gade M, Sangabathuni S, Thulasiram HV, Kikkeri R (2017) Exploring the influence of shapes and heterogeneity of glyco-gold nanoparticles on bacterial binding for preventing infections. Chem Med Chem 12(14):1116–1124. https://doi.org/10.1002/cmdc.201700218CrossRef

85.

Pelicano H, Martin DS, Xu RH, Huang P (2006) Glycolysis inhibition for anticancer treatment. Oncogene 25:4633–4646. https://doi.org/10.1038/sj.onc.1209597CrossRef

86.

Alnashiri HM, Aldakheel FM, Binshaya AS, Alharthi NS, Ahmed M (2022) Antimicrobial analysis of biosynthesized lectin-conjugated gold nanoparticles. Adsorp Sci Technol 8187260. https://doi.org/10.1155/2022/8187260

87.

Barboiu M, Mouline Z, Silion M et al (2014) Multivalent recognition of concanavalin A by Mo₁₃₂ glyconanocapsules—toward biomimetic hybrid multilayers. Chemistry 20:6678–6683. https://doi.org/10.1002/chem.201402187CrossRef

88.

Chao Y, Karmali PP, Simberg D (2012) Role of carbohydrate receptors in the macrophage uptake of dextran-coated iron oxide nanoparticles. Adv Exp Med Biol 733:115–123. https://doi.org/10.1007/978-94-007-2555-3_11CrossRef

89.

Thomas SC, Harshita MPK et al (2015) Ceramic nanoparticles: fabrication methods and applications in drug delivery. Curr Pharm Des 21:6165–6188CrossRef

90.

Rawat M, Singh D, Saraf S et al (2006) Nanocarriers: promising vehicle for bioactive drugs. Biol Pharm Bull 29:1790–1798. https://doi.org/10.1248/bpb.29.1790CrossRef

91.

Jores K, Mehnert W, Drechsler M et al (2004) Investigations on the structure of solid lipid nanoparticles (SLN) and oil-loaded solid lipid nanoparticles by photon correlation spectroscopy, field-flow fractionation and transmission electron microscopy. J Control Release 95:217–227. https://doi.org/10.1016/j.jconrel.2003.11.012CrossRef

92.

Gradishar WJ, Tjulandin S, Davidson N et al (2005) Phase III trial of nanoparticle albumin-bound paclitaxel compared with polyethylated castor oil-based paclitaxel in women with breast cancer. J Clin Oncol 23:7794–7803. https://doi.org/10.1200/JCO.2005.04.937CrossRef

93.

Sabbatini P, Aghajanian C, Dizon D et al (2004) Phase II study of CT-2103 in patients with recurrent epithelial ovarian, fallopian tube, or primary peritoneal carcinoma. J Clin Oncol 22:4523–4531. https://doi.org/10.1200/JCO.2004.12.043CrossRef

94.

Bhatt R, de Vries P, Tulinsky J et al (2003) Synthesis and in vivo antitumor activity of poly(l-glutamic acid) conjugates of 20S-camptothecin. J Med Chem 46:190–193. https://doi.org/10.1021/jm020022rCrossRef

95.

Duncan R (2003) The dawning era of polymer therapeutics. Nat Rev Drug Discov 2:347–360. https://doi.org/10.1038/nrd1088CrossRef

96.

Chen Y, Liu L (2012) Modern methods for delivery of drugs across the blood-brain barrier. Adv Drug Deliv Rev 64:640–665. https://doi.org/10.1016/j.addr.2011.11.010CrossRef

97.

Mohamed F, van der Walle CF (2008) Engineering biodegradable polyester particles with specific drug targeting and drug release properties. J Pharm Sci 97:71–87. https://doi.org/10.1002/jps.21082CrossRef

98.

Pillay S, Pillay V, Choonara YE et al (2009) Design, biometric simulation and optimization of a nano-enabled scaffold device for enhanced delivery of dopamine to the brain. Int J Pharm 382:277–290. https://doi.org/10.1016/j.ijpharm.2009.08.021CrossRef

99.

Chen J, Zhang C, Liu Q et al (2012) Solanum tuberosum lectin-conjugated PLGA nanoparticles for nose-to-brain delivery: in vivo and in vitro evaluations. J Drug Target 20:174–184. https://doi.org/10.3109/1061186X.2011.622396CrossRef

100.

Yang R, Xu J, Xu L et al (2018) Cancer cell membrane-coated adjuvant nanoparticles with mannose modification for effective anticancer vaccination. ACS Nano 26:5121–5129. https://doi.org/10.1021/acsnano.7b09041CrossRef

101.

Wu G, Zhou F, Ge L et al (2012) Novel mannan-PEG-PE modified bio adhesive PLGA nanoparticles for targeted gene delivery. J Nanomaterials 2012:981670. https://doi.org/10.1155/2012/981670CrossRef

102.

El-Hammadi MM, Arias JL (2022) Recent advances in the surface functionalization of PLGA-based nanomedicines. Nanomaterials 12:354. https://doi.org/10.3390/nano12030354CrossRef

103.

Nasongkla N, Bey E, Ren J, Ai H et al (2006) Multifunctional polymeric micelles as cancer-targeted MRI-ultrasensitive drug delivery systems. Nano Lett 6:2427–2430. https://doi.org/10.1021/nl061412uCrossRef

104.

Heller P, Mohr N, Birke A et al (2015) Directed interactions of block copolypept(o)ides with mannose-binding receptors: PeptoMicelles targeted to cells of the innate immune system. Macromol Biosci 15:63–73. https://doi.org/10.1002/mabi.201400417CrossRef

105.

Svenson S, Tomalia DA (2005) Dendrimers in biomedical applications—reflections on the field. Adv Drug Deliv Rev 57:2106–2129. https://doi.org/10.1016/j.addr.2005.09.018CrossRef

106.

Lee CC, Gillies ER, Fox ME et al (2006) A single dose of doxorubicin-functionalized bow-tie dendrimer cures mice bearing C-26 colon carcinomas. Proc Natl Acad Sci USA 103:16649–16654. https://doi.org/10.1073/pnas.0607705103CrossRef

107.

Sehad C, Shiao TC, Sallam LM et al (2018) Effect of dendrimer generation and aglyconic linkers on the binding properties of mannosylated dendrimers prepared by a combined convergent and onion peel approach. Molecules 23(8):1890. https://doi.org/10.3390/molecules23081890CrossRef

108.

Martos-Maldonado MC, Casas-Solvas JM, Quesada-Soriano I et al (2013) Poly(amido amine)-based mannose-glycodendrimers as multielectron redox probes for improving lectin sensing. Langmuir 29:1318–1326. https://doi.org/10.1021/la304107aCrossRef

109.

Kikkeri R, Grünstein D, Seeberger PH (2010) Lectin biosensing using digital analysis of Ru(II)-glycodendrimers. J Am Chem Soc 132:10230–10232CrossRef

110.

Giddam AK, Zaman M, Skwarczynski M et al (2012) Liposome-based delivery system for vaccine candidates: constructing an effective formulation. Nanomedicine 7:1877–1893. https://doi.org/10.2217/nnm.12.157CrossRef

111.

Jain KK (2005) Nanotechnology in clinical laboratory diagnostics. Clin Chim Acta 358:37–54. https://doi.org/10.1016/j.cccn.2005.03.014CrossRef

112.

Nisini R, Poerio N, Mariotti S et al (2018) The multirole of liposomes in therapy and prevention of infectious diseases. Front Immunol. https://doi.org/10.3389/fimmu.2018.00155CrossRef

113.

Gorelik E, Galili U, Raz A (2001) On the role of cell surface carbohydrates and their binding proteins (lectins) in tumor metastasis. Cancer Metastasis Rev 20:245–277. https://doi.org/10.1023/a:1015535427597CrossRef

114.

Gabor F, Bogner E, Weissenboeck A et al (2004) The lectin-cell interaction and its implications to intestinal lectin-mediated drug delivery. Adv Drug Deliv Rev 56:459–480. https://doi.org/10.1016/j.addr.2003.10.015CrossRef

115.

Dekel R, Zvibel I, Brill S et al (2003) Gliotoxin ameliorates development of fibrosis and cirrhosis in a thioacetamide rat model. Dig Dis Sci 48:1642–1647. https://doi.org/10.1023/a:1024792529601CrossRef

116.

Yewale C, Baradia D, Vhora I et al (2013) Proteins: emerging carrier for delivery of cancer therapeutics. Expert Opin Drug Deliv 10:1429–1448. https://doi.org/10.1517/17425247.2013.805200CrossRef

117.

Gradishar WJ, Tjulandin S, Davidson N et al (2005) Phase III trial of NP albumin-bound paclitaxel compared with polyethylated castor oil-based paclitaxel in women with breast cancer. J Clin Oncol 23:7794–7803. https://doi.org/10.1200/JCO.2005.04.937CrossRef

118.

Kang YJ, Yang HJ, Jeon S et al (2014) Polyvalent display of monosaccharides on ferritin protein cage NPs for the recognition and binding of cell-surface lectins. Macromol Biosci 14:619–625. https://doi.org/10.1002/mabi.201300528CrossRef

119.

Hussain N, Jani PU, Florence AT (1997) Enhanced oral uptake of tomato lectin-conjugated nanoparticles in the Rat. Pharm Res 14:613–618. https://doi.org/10.1023/a:1012153011884CrossRef

120.

Kasuya T, Jung J, Kadoya H et al (2008) In vivo delivery of bionanocapsules displaying Phaseolus vulgaris agglutinin-L4 isolectin to malignant tumors overexpressing N-acetylglucosaminyl transferase V. Hum Gene Ther 19:887–895. https://doi.org/10.1089/hum.2008.037CrossRef

121.

Robinson MA, Charlton ST, Garnier P et al (2004) LEAPT: lectin-directed enzyme-activated prodrug therapy. Proc Natl Acad Sci USA 101:14527–14532. https://doi.org/10.1073/pnas.0303574101CrossRef

122.

Gao X, Chen J, Tao W et al (2007) UEA I-bearing NPs for brain delivery following intranasal administration. Int J Pharm 340:207–215. https://doi.org/10.1016/j.ijpharm.2007.03.039CrossRef

123.

Bies V, Lehr CM, Woodley JF (2004) Lectin-mediated drug targeting: history and applications. Adv Drug Deliv Rev 56:425–435. https://doi.org/10.1016/j.addr.2003.10.030CrossRef

124.

Nishiyama K, Takakusagi Y, Kusayanagi T et al (2009) Identification of trimannoside-recognizing peptide sequences from a T7 phage display screen using a QCM device. Bioorg Med Chem 17:195–202. https://doi.org/10.1016/j.bmc.2008.11.004CrossRef

125.

McNicholas S, Rencurosi A, Lay L et al (2007) Amphiphilic N-glycosyl-thiocarbamoyl cyclodextrins: synthesis, self-assembly, and fluorimetry of recognition by Lens culinaris lectin. Biomacromol 8:1851–1857. https://doi.org/10.1021/bm070055uCrossRef

126.

Pusztai A, Grant G, Spencer RJ et al (1993) Kidney bean lectin-induced Escherichia coli overgrowth in the small intestine is blocked by GNA, a mannose-specific lectin. J Appl Bacteriol 75:360–368. https://doi.org/10.1111/j.1365-2672.1993.tb02788.xCrossRef

127.

Branderhorst HM, Ruijtenbeek R, Liskamp RMJ et al (2008) Multivalent carbohydrate recognition on a glycodendrimer-functionalized flow-through chip. ChemBioChem 9:1836–1844. https://doi.org/10.1002/cbic.200800195CrossRef

128.

Kong JE, Kahkeshani S, Pushkarsky I et al (2014) Research highlights: micro-engineered therapies. Lab Chip 14:4585–4589. https://doi.org/10.1039/c4lc90107jCrossRef

129.

Budhadev D, Poole E, Nehlmeier I et al (2020) Glycan-gold nanoparticles as multifunctional probes for multivalent lectin–carbohydrate binding: implications for blocking virus infection and nanoparticle assembly. J Am Chem Soc 142:18022–18034. https://doi.org/10.1021/jacs.0c06793CrossRef

130.

Jirátová M, Gálisová A, Rabyk M et al (2020) Mannan-based nanodiagnostic agents for targeting sentinel lymph nodes and tumors. Molecules 26:146. https://doi.org/10.3390/molecules26010146CrossRef

131.

Zhang C, Qu X, Li J et al (2015) Biofabricated NP coating for liver-cell targeting. Adv Healthc Mater 4:1972–1981. https://doi.org/10.1002/adhm.201500202CrossRef

132.

Shao X, Liu Q, Zhang C et al (2013) Concanavalin A-conjugated poly(ethylene glycol)-poly(lactic acid) NPs for intranasal drug delivery to the cervical lymph nodes. J Microencapsul 30:780–786. https://doi.org/10.3109/02652048.2013.788086CrossRef

133.

Ali M, Ramirez P, Tahir MN et al (2011) Biomolecular conjugation inside synthetic polymer nanopores via glycoprotein-lectin interactions. Nanoscale 3:1894–1903. https://doi.org/10.1039/c1nr00003aCrossRef

134.

Zhang N, Ping QN, Huang GH et al (2005) Investigation of lectin-modified insulin liposomes as carriers for oral administration. Int J Pharm 295:247–259. https://doi.org/10.1016/j.ijpharm.2005.01.018CrossRef

135.

Zhang N, Ping QN, Huang GH et al (2006) Lectin-modified solid lipid nanoparticles as carriers for oral administration of insulin. Int J Pharm 327:153–159. https://doi.org/10.1016/j.ijpharm.2006.07.026CrossRef

136.

Miyake A, Akagi T, Enose Y et al (2004) Induction of HIV-specific antibody response and protection against vaginal transmission by intranasal immunization with inactivated -capturing nanospheres in macaques. J Med Virol 73:368–377. https://doi.org/10.1002/jmv.20100CrossRef

137.

Moulari B, Béduneau V, Lamprecht A (2014) Lectin-decorated NPs enhance binding to the inflamed tissue in experimental colitis. Control Release 188:9–17. https://doi.org/10.1016/j.jconrel.2014.05.046CrossRef

138.

Ulbrich W, Lamprecht A (2010) Targeted drug-delivery approaches by nanoparticulate carriers in the therapy of inflammatory diseases. J R Soc Interface 7:S55–S66. https://doi.org/10.1098/rsif.2009.0285.focusCrossRef

139.

Varshosaz J, Moazen E (2014) Novel lectin-modified poly[ethylene-co-vinyl acetate] mucoadhesive NPs of carvedilol: preparation and in vitro optimization using a two-level factorial design. Pharm Dev Technol 19:605–617. https://doi.org/10.3109/10837450.2013.819011CrossRef

140.

Umamaheshwari RB, Jain NK (2003) Receptor mediated targeting of lectin conjugated gliadin NPs in the treatment of Helicobacter pylori. J Drug Target 11:415–423. https://doi.org/10.1080/10611860310001647771CrossRef

141.

Bahrami B, Hojjat-Farsangi M, Mohammadi H et al (2017) NPs and targeted drug delivery in cancer therapy. Immunol Lett 190:64–83. https://doi.org/10.3389/fmolb.2020.00193CrossRef

142.

Makky A, Michel JP, Kasselouri A et al (2010) Evaluation of the specific interactions between glycodendrimeric porphyrins, free or incorporated into liposomes, and concanavalin A by fluorescence spectroscopy, surface pressure and QCM-D measurements. Langmuir 26:12761–12768. https://doi.org/10.1021/la101260tCrossRef

143.

Staegemann MH, Gitter B, Dernedde J et al (2017) Mannose-functionalized hyperbranched polyglycerol loaded with zinc porphyrin: investigation of the multivalency effect in antibacterial photodynamic therapy. Chemistry 23:3918–3930. https://doi.org/10.1002/chem.201605236CrossRef

144.

Vossen L, Asenjo BD, Gutiérrez-Corbo C et al (2020) Mannose-decorated dendritic polyglycerol nanocarriers drive antiparasitic drugs to Leishmania infantum-infected macrophages. Pharmaceutics 24:915. https://doi.org/10.3390/pharmaceutics12100915CrossRef

145.

Ben ER, Barragán TM, de Dionisio EG et al (2019) Mannose-coated polydiacetylene (PDA)-based nanomicelles: synthesis, interaction with concanavalin A and application in the water solubilization and delivery of hydrophobic molecules. J Mater Chem B 7:5930–5946. https://doi.org/10.1039/C9TB01218DCrossRef

146.

Irache JM, Salman HH, Gamazo C et al (2008) Mannose-targeted systems for the delivery of therapeutics. Expert Opin Drug Deliv 5:703–724. https://doi.org/10.1517/17425247.5.6.703CrossRef

147.

Cuenca AG, Jiang H, Hochwald SN et al (2006) Emerging implications of nanotechnology on cancer diagnostics and therapeutics. Cancer 107:459–466. https://doi.org/10.1002/cncr.22035CrossRef

148.

Budzynska R, Nevozhay D, Kanska U et al (2007) Antitumor activity of mannan-methotrexate conjugate in vitro and in vivo. Oncol Res 16:415–421. https://doi.org/10.3727/000000007783980837CrossRef

149.

Tokatlian T, Read BJ, Jones CA et al (2019) Innate immune recognition of glycans targets HIV nanoparticle immunogens to germinal centres. Science 363:649–654. https://doi.org/10.1126/science.aat9120CrossRef

150.

Liang WW, Shi X, Deshpande D et al (1996) Oligonucleotide targeting to alveolar macrophages by mannose receptor-mediated endocytosis. Biochim Biophys Acta 1279:227–234. https://doi.org/10.1016/0005-2736(95)00237-5CrossRef

151.

Wijagkanalan W, Kawakami S, Takenaga M et al (2008) Efficient targeting to alveolar macrophages by intratracheal administration of mannosylated liposomes in rats. J Control Release 125:121–130. https://doi.org/10.1016/j.jconrel.2007.10.011CrossRef

152.

Grandjean C, Angyalosi G, Loing E et al (2001) Novel hyperbranched glycomimetics recognized by the human mannose receptor: quinic or shikimic acid derivatives as mannose bioisosteres. ChemBioChem 2:747–757. https://doi.org/10.1002/1439-7633(20011001)2:10%3c747::AID-CBIC747%3e3.0.CO;2-OCrossRef

153.

Choi M, Choi SJ, Jang S et al (2019) Shikimic acid, a mannose bioisostere, promotes hair growth with the induction of anagen hair cycle. Sci Rep 9:17008. https://doi.org/10.1038/s41598-019-53612-5CrossRef

154.

Gac S, Coudane J, Boustta M et al (2000) Synthesis, characterisation and in vivo behaviour of a norfloxacin-poly[L-lysine citramide imide] conjugate bearing mannosyl residues. J Drug Target 7:393–406CrossRef

155.

Diebold SS, Kursa M, Wagner E et al (1999) Mannose polyethylenimine conjugates for targeted DNA delivery into dendritic cells. J Biol Chem 274:19087–19094. https://doi.org/10.1074/jbc.274.27.19087CrossRef

156.

Dutta T, Jain NK (2007) Targeting potential and anti-HIV activity of lamivudine loaded mannosylated poly [propyleneimine] dendrimer. Biochim Biophys Acta 1770:681–686. https://doi.org/10.1016/j.bbagen.2006.12.007CrossRef

157.

Park IY, Kim IY, Yoo MK et al (2008) Mannosylated polyethylenimine coupled mesoporous silica NPs for receptor-mediated gene delivery. Int J Pharm 359:280–287. https://doi.org/10.1016/j.ijpharm.2008.04.010CrossRef

158.

Park KH, Sung WJ, Kim S et al (2005) Specific interaction of mannosylated glycopolymers with macrophage cells mediated by mannose receptor. J Biosci Bioeng 99:285–289. https://doi.org/10.1263/jbb.99.285CrossRef

159.

Fromell K, Andersson M, Elihn K et al (2005) NP decorated surfaces with potential use in glycosylation analysis. Colloids Surf B Biointerfaces 46:84–91. https://doi.org/10.1016/j.colsurfb.2005.06.017CrossRef

160.

Serizawa T, Yasunaga S, Akashi M (2001) Synthesis and lectin recognition of polystyrene core-glycopolymer corona nanospheres. Biomacromol 2:469–475. https://doi.org/10.1021/bm000131sCrossRef

161.

Lee YS, Park KH, Kim TS et al (2008) Interaction of glycopolymers with human hematopoietic cells from cord blood and peripheral blood. J Biomed Mater Res A 86:1069–1076. https://doi.org/10.1002/jbm.a.31743CrossRef

162.

Ahire JH, Chambrier I, Mueller A et al (2013) Synthesis of D-mannose capped silicon NPs and their interactions with MCF-7 human breast cancerous cells. ACS Appl Mater Interfaces 5:7384–7391. https://doi.org/10.1021/am4017126CrossRef

163.

Štimac A, Cvitaš VL, Frkanec L et al (2016) Design, and syntheses of mono and multivalent mannosyl-lipoconjugates for targeted liposomal drug delivery. Int J Pharm 511:44–56. https://doi.org/10.1016/j.ijpharm.2016.06.123CrossRef

164.

Witoonsaridsilp W, Paeratakul V, Panyarachun B et al (2012) Development of mannosylated liposomes using synthesized N-octadecyl-D-mannopyranosylamine to enhance gastrointestinal permeability for protein delivery. AAPS Pharm Sci Tech 13:699–706. https://doi.org/10.1208/s12249-012-9788-1CrossRef

165.

Mitra M, Mandal AK, Chatterjee TK et al (2005) Targeting of mannosylated liposome incorporated benzyl derivative of Penicillium nigricans derived compound MT81 to reticuloendothelial systems for the treatment of visceral leishmaniasis. J Drug Target 13:285–293. https://doi.org/10.1080/10611860500233306CrossRef

166.

Garg M, Asthana A, Agashe HB et al (2006) Stavudine-loaded mannosylated liposomes: in-vitro anti-HIV-I activity, tissue distribution and pharmacokinetics. J Pharm Pharmaco 58:605–616. https://doi.org/10.1211/jpp.58.5.0005CrossRef

167.

Kaur CD, Nahar M, Jain NK (2009) Lymphatic targeting of zidovudine using surface-engineered liposomes. J Drug Target 16:798–805. https://doi.org/10.1080/10611860802475688CrossRef

168.

Zhang Y, Li H, Sun J et al (2010) C-Chol/DOPE cationic liposomes: a comparative study of the influence factors on plasmid pDNA and siRNA gene delivery. Int J Pharm 390:198–207. https://doi.org/10.1016/j.ijpharm.2010.01.035CrossRef

169.

Ozpolat B, Sood AK, Lopez-Berestein G (2014) Liposomal siRNA nanocarriers for cancer therapy. Adv Drug Deliv Rev 66:110–116. https://doi.org/10.1016/j.addr.2013.12.008CrossRef

170.

Yeeprae W, Kawakami S, Yamashita F et al (2006) Effect of mannose density on mannose receptor-mediated cellular uptake of mannosylated O/W emulsions by macrophages. J Control Release 114:193–201. https://doi.org/10.1016/j.jconrel.2006.04.010CrossRef

171.

Kuramoto Y, Kawakami S, Zhou S et al (2008) Use of mannosylated cationic liposomes/ immunostimulatory CpG DNA complex for effective inhibition of peritoneal dissemination in mice. J Gene Med 10:392–399. https://doi.org/10.1002/jgm.1162CrossRef

172.

Ruan GX, Chen YZ, Yao XL et al (2014) Macrophage mannose receptor-specific gene delivery vehicle for macrophage engineering. Acta Biomater 10:1847–1855. https://doi.org/10.1016/j.actbio.2014.01.012CrossRef

173.

Wang N, Wang T, Zhang M et al (2014) Mannose derivative and lipid A dually decorated cationic liposomes as an effective cold chain free oral mucosal vaccine adjuvant-delivery system. Eur J Pharm Biopharm 88:194–206. https://doi.org/10.1016/j.ejpb.2014.04.007CrossRef

174.

Bartheldyová E, Knotigová PT, Zachová K et al (2019) N-Oxy lipid-based click chemistry for orthogonal coupling of mannan onto nanoliposomes prepared by microfluidic mixing: synthesis of lipids, characterisation of mannan-coated nanoliposomes and in vitro stimulation of dendritic cells. Carbohydr Polym 207:521–532. https://doi.org/10.1016/j.carbpol.2018.10.121CrossRef

175.

Bru¨ck A, Abu-Dahab R, Borchard G et al (2001) Lectin-functionalized liposomes for pulmonary drug delivery: interaction with human alveolar epithelial cells. J Drug Targeting 9:241–251. https://doi.org/10.3109/10611860108997933CrossRef

176.

Lloyd MG, Liu D, Legendre M et al (2022) H84T BanLec has broad spectrum antiviral activity against human herpesviruses in cells, skin, and mice. Sci Rep 12:1641. https://doi.org/10.1038/s41598-022-05580-6CrossRef

177.

Covés-Datson EM, King SR, Legendre M et al (2021) Targeted disruption of pi-pi stacking in Malaysian banana lectin reduces mitogenicity while preserving antiviral activity. Sci Rep 11:656. https://doi.org/10.1038/s41598-020-80577-7CrossRef

178.

Christodoulou I, RahnamaRavich R et al (2021) Glycoprotein targeted CAR-NK cells for the treatment of SARS-CoV-2 infection. Front Immunol 12:763460. https://doi.org/10.3389/fimmu.2021.763460CrossRef

179.

dos Santos MA, Grenha A (2015) Polysaccharide NPs for protein and peptide delivery: exploring less-known materials. Adv Protein Chem Struct Biol 98:223–261. https://doi.org/10.1016/bs.apcsb.2014.11.003CrossRef

180.

Ye Z, Zhang Q, Wang S et al (2016) Tumour-targeted drug delivery with mannose-functionalized nanoparticles self-assembled from amphiphilic b-cyclodextrins. Chem Eur 22:15216–15221. https://doi.org/10.1002/chem.201603294CrossRef

181.

Lemarchanda C, Gref R, Couvreura P (2004) Polysaccharide-decorated NPs. Eur J Pharma Biopharma 58:327–341. https://doi.org/10.1016/j.ejpb.2004.02.016CrossRef

182.

Yao W, Peng Y, Du M et al (2013) Preventative vaccine-loaded mannosylated chitosan NPs intended for nasal mucosal delivery enhance immune responses and potent tumor immunity. Mol Pharm 10:2904–2914. https://doi.org/10.1021/acs.molpharmaceut.7b00278CrossRef

183.

Yasin U, Bilal M, Bashir H et al (2020) Preparation and nanoencapsulation of lectin from Lepidium sativum on chitosan-tripolyphosphate nanoparticle and their cytotoxicity against hepatocellular carcinoma cells (HepG2). BioMed Res Inter 2020:7251346. https://doi.org/10.1155/2020/7251346CrossRef

184.

Shahnaz G, Edagwa BJ, McMillan J et al (2017) Development of mannose-anchored thiolated amphotericin B nanocarriers for treatment of visceral leishmaniasis. Nanomedicine 12:99–115. https://doi.org/10.2217/nnm-2016-0325CrossRef

185.

Mukhtar M, Zeeshan M, Khan S et al (2020) Fabrication and optimization of pH-sensitive mannose-anchored nano-vehicle as a promising approach for macrophage uptake. App Nanosci 10:4013–4027CrossRef

186.

Liu P, Gao C, Chen H et al (2021) Receptor-mediated targeted drug delivery systems for treatment of inflammatory bowel disease: opportunities and emerging strategies. Acta pharmaceutica Sinica B 11:2798–2818. https://doi.org/10.1016/j.apsb.2020.11.003CrossRef

187.

Renu S, Feliciano-Ruiz N, Patil V et al (2021) Immunity and protective efficacy of mannose conjugated chitosan-based influenza nanovaccine in maternal antibody positive pigs. Front Immunol 12:584299. https://doi.org/10.3389/fimmu.202CrossRef

188.

Hatami E, Mu Y, Shields DN et al (2019) Mannose-decorated hybrid nanoparticles for enhanced macrophage targeting. Biochem Biophys Rep 17:197–207. https://doi.org/10.1016/j.bbrep.2019.01.007CrossRef

189.

Sathiyaseelan A, Saravanakumar K, Mariadoss AVA et al (2021) Antimicrobial and wound healing properties of FeO fabricated chitosan/PVA nanocomposite sponge. Antibiotics 10:524. https://doi.org/10.3390/antibiotics10050524CrossRef

190.

Rho JG, Han HS, Han JH et al (2018) Self-assembled hyaluronic acid NPs: implications as a nanomedicine for treatment of type 2 diabetes. J Control Release 279:89–98. https://doi.org/10.1016/j.jconrel.2018.04.006CrossRef

191.

Gennari A, Pelliccia M, Donno R et al (2016) Mannosylation allows for synergic (CD44/C-type lectin) uptake of hyaluronic acid NPs in dendritic cells, but only upon correct ligand presentation. Adv Healthc Mater 5:966–976. https://doi.org/10.1002/adhm.201500941CrossRef

192.

Spadea A, Rios de la Rosa JM et al (2019) Evaluating the efficiency of hyaluronic acid for tumor targeting via CD44. Mol Pharm 16:2481–2493. https://doi.org/10.1021/acs.molpharmaceut.9b00083CrossRef

193.

Tian G, Sun X, Bai J et al (2019) Doxorubicin-loaded dual-functional hyaluronic acid NPs: preparation, characterization, and antitumor efficacy in vitro and in vivo. Mol Med Rep 19:133–142. https://doi.org/10.3892/mmr.2018.9687CrossRef

194.

Lallana E, Rios de la Rosa JM et al (2017) Chitosan/hyaluronic acid NPs: rational design revisited for RNA delivery. Mol Pharm 14:2422–2436. https://doi.org/10.1021/acs.molpharmaceut.7b00320CrossRef

195.

Yoon HY, Koo H, Choi KY et al (2012) Tumor-targeting hyaluronic acid NPs for photodynamic imaging and therapy. Biomaterials 33:3980–3989. https://doi.org/10.1016/j.biomaterials.2012.02.016CrossRef

196.

Nanda RK, Hajam IA, Edao BM et al (2014) Immunological evaluation of mannosylated chitosan NPs based foot and mouth disease virus DNA vaccine, pVAC FMDV VP1-OmpA in guinea pigs. Biologicals 42:153–159. https://doi.org/10.1016/j.biologicals.2014.01.002CrossRef

197.

Rodriguez-Torres M, Acosta-Torres LS, Diaz-Torres LA (2018) Heparin-based NPs: an overview of their applications. J Nanomaterials 2018:9780489. https://doi.org/10.1155/2018/9780489CrossRef

198.

She W, Li N, Luo K et al (2013) Dendronized heparin-doxorubicin conjugate-based NP as pH-responsive drug delivery system for cancer therapy. Biomaterials 34:2252–2264. https://doi.org/10.1016/j.biomaterials.2012.12.017CrossRef

199.

Wu W, Yao W, Wang X et al (2015) Bioreducible heparin-based nanogel drug delivery system. Biomaterials 39:260–268. https://doi.org/10.1016/j.biomaterials.2014.11.005CrossRef

200.

Ismaya WT, Tjandrawinata RR, Rachmawati H (2020) Lectins from edible mushroom Agaricus bisporus and their therapeutic potentials. Molecules 25:2368. https://doi.org/10.3390/molecules25102368CrossRef

201.

Benito JM, Gomez-Garcia M, Mellet CO et al (2004) Optimizing saccharide-directed molecular delivery to biological receptors: design, synthesis, and biological evaluation of glycodendrimer-cyclodextrin conjugates. J Am Chem Soc 126:10355–10363. https://doi.org/10.1021/ja047864vCrossRef

202.

Rieger J, Stoffelbach F, Cui D et al (2007) Mannosylated poly[ethylene oxide]-b-poly[epsilon-caprolactone] diblock copolymers: synthesis, characterization and interaction with a bacterial lectin. Biomacromol 8:2717–2725. https://doi.org/10.1021/bm070342yCrossRef

203.

Alvarez-Manceñido F, Landin M, Lacik I et al (2008) Konjac glucomannan and konjac glucomannan/xanthan gum mixtures as excipients for controlled drug delivery systems. Diffusion of small drugs. Int J Pharm 349:11–18. https://doi.org/10.1016/j.ijpharm.2007.07.015CrossRef

204.

Alvarez-Manceñido F, Landin M, Martínez-Pacheco R (2008) Konjac glucomannan/xanthan gum enzyme sensitive binary mixtures for colonic drug delivery. Eur J Pharm Biopharm 69:573–581. https://doi.org/10.1016/j.ejpb.2008.01.004CrossRef

205.

Singh V, Sethi R, Tiwari A (2009) Structure elucidation and properties of a non-ionic galactomannan derived from the Cassia pleurocarpa seeds. Int J Biol Macromo 44:9–13. https://doi.org/10.1016/j.ijbiomac.2008.09.012CrossRef

206.

Alves A, Miguel SP, Araujo ARTS et al (2020) Xanthan gum–konjac glucomannan blend hydrogel for wound healing. Polymers 12:99. https://doi.org/10.3390/polym12010099CrossRef

207.

Ruge CA, Hillaireau H, Grabowski N et al (2016) Pulmonary surfactant protein A-mediated enrichment of surface-decorated polymeric nanoparticles in alveolar macrophages. Mol Pharm 13:4168–4178. https://doi.org/10.1021/acs.molpharmaceut.6b00773CrossRef

208.

Pongrac IM, Radmilović MD, Ahmed LB et al (2019) D-mannose-Coating of maghemite nanoparticles improved labeling of neural stem cells and allowed their visualization by ex vivo MRI after transplantation in the mouse brain. Cell Transplant 28:553–567. https://doi.org/10.1177/0963689719834304CrossRef

Title: Applications of mannose-binding lectins and mannan glycoconjugates in nanomedicine
Authors: Anita Gupta
G. S. Gupta
Publication date: 01-11-2022
Publisher: Springer Netherlands
Published in: Journal of Nanoparticle Research / Issue 11/2022
Print ISSN: 1388-0764
Electronic ISSN: 1572-896X
DOI: https://doi.org/10.1007/s11051-022-05594-1

Springer Professional

Abstract

Graphical abstract

Please log in to get access to your license.

Dont have a licence yet? Then find out more about our products and how to get one now:

Springer Professional "Wirtschaft+Technik"

Springer Professional "Technik"

Other articles of this Issue 11/2022

An aqueous ammonia detection by hybrid Ag-CdS quantum dots

Review article on the performance of electrochemical capacitors when altered metals doped with nickel oxide nanomaterials

Highly sensitive non-enzymatic glucose sensor based on copper oxide nanorods

Structural, electronic, and elastic properties of different polytypes of GaSe lamellar materials under compressive stress: insights from a DFT study

A study on effect of MgO nanoparticles loading on the electrical conducting properties of polyvinyl alcohol/polyaniline polymer composite films

Electrodeposited CuSbSe2 thin films based solar cells on various substrates

Premium Partners