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Erschienen in:

2017 | OriginalPaper | Buchkapitel

Oligooxopiperazines as Topographical Helix Mimetics

verfasst von : Brooke Bullock Lao, Paramjit S. Arora

Erschienen in: Peptidomimetics II

Verlag: Springer International Publishing

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Abstract

Protein–protein interactions are often mediated by amino acid side chain functionality organized on secondary structures. Small molecule scaffolds that reproduce the array of protein-like functionality at interfaces offer an attractive approach to target therapeutically important interactions. Here, we describe the design, synthesis, and the biological potential of small molecule helix mimetics derived from an oxopiperazine scaffold to target protein complexes in which binding is largely dictated by one face of the interfacial helix. The oxopiperazine helix mimetics can be assembled from α-amino acids using standard solid-phase peptide synthesis methodology, enabling rapid diversification of the scaffold and discovery of ligands for protein targets. We have evaluated the biological potential of the oxopiperazine mimetics in cell-free, cell culture, and in vivo models. Our results support the hypothesis that the scaffold offers an attractive platform for the development of novel inhibitors of protein–protein interactions.

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Titel: Oligooxopiperazines as Topographical Helix Mimetics
verfasst von: Brooke Bullock Lao
Paramjit S. Arora
Verlag: Springer International Publishing
Buch: Peptidomimetics II
Print ISBN: 978-3-319-49123-3

Electronic ISBN: 978-3-319-49124-0

Copyright-Jahr: 2017
DOI: https://doi.org/10.1007/7081_2015_195