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Title

Evolution in non-peptide α-helix mimetics on the road to effective protein-protein interaction modulators

AuthorsMartín-Martínez, Mercedes ; González-Muñiz, Rosario ; Algar, Sergio
KeywordsProtein-protein interactions
Non-peptide α-helix mimetics
Proteomimetics
Small-molecules
Issue Date2021
PublisherElsevier
CitationEuropean Journal of Medicinal Chemistry 211: 1-18 (2021)
AbstractModulation of interactome networks, essentially protein-protein interactions (PPIs), might representvaluable therapeutic approaches to different pathological conditions. Since a high percentage of PPIs aremediated bya-helical structures at the interacting surface, the development of compounds able toreproduce the amino acid side-chain organization ofa-helices (e.g. stabilizeda-helix peptides andb-derivatives, proteomimetics, anda-helix small-molecule mimetics) focuses the attention of differentresearch groups. This appraisal describes the recent progress in the non-peptidea-helix mimeticsfield,which has evolved from single-face to multi-face reproducing compounds and from oligomeric tomonomeric scaffolds able to bear different substituents in similar spatial dispositions as the side-chainsin canonical helices. Grouped by chemical structures, the review contemplates terphenyl-like molecules,oligobenzamides and heterocyclic analogues, benzamide-amino acid conjugates and non-oligomericsmall-molecules mimetics, among others, and their effectiveness to stabilize/disrupt therapeuticallyrelevant PPIs. The X-ray structures of a couple of oligomeric peptidomimetics and of some small-molecules complexed with the MDM2 protein, as well as the state of the art on their development inclinical trials, are also remarked. The discovery of a continuously increasing number of new disease-relevant PPIs could offer future opportunities for these and other forthcominga-helix mimetics.
Publisher version (URL)http://dx.doi.org/10.1016/j.ejmech.2020.113015
URIhttp://hdl.handle.net/10261/240965
Identifiersdoi: 10.1016/j.ejmech.2020.113015
issn: 0223-5234
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