@inbook{3d43729d484a4d32af893eb33005a136,
title = "α-Helix mimicry with α/β-peptides",
abstract = "We describe a general strategy for creating peptidic oligomers that have unnatural backbones but nevertheless adopt a conformation very similar to the α-helix. These oligomers contain both α- and β-amino acid residues (α/β-peptides). If the β content reaches 25-30% of the residue total, and the β residues are evenly distributed along the backbone, then substantial resistance to proteolytic degradation is often observed. These α/β-peptides can mimic the informational properties of α-helices involved in protein-protein recognition events, as documented in numerous crystal structures. Thus, these unnatural oligomers can be a source of antagonists of undesirable protein-protein interactions that are mediated by natural α-helices, or agonists of receptors for which the natural polypeptide ligands are α-helical. Successes include mimicry of BH3 domains found in proapoptotic proteins, which leads to ligands for antiapoptotic Bcl-2 family proteins, and mimicry of the gp41 CHR domain, which leads to inhibition of HIV infection in cell-based assays.",
keywords = "Alpha-helix mimicry, Alpha/beta-peptides, BH3 domain, Beta-peptides, Foldamers, Protein-protein interactions, gp41 HIV",
author = "Johnson, {Lisa M.} and Gellman, {Samuel H.}",
year = "2013",
doi = "10.1016/B978-0-12-394292-0.00019-9",
language = "English (US)",
isbn = "9780123942920",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "407--429",
booktitle = "Methods in Protein Design",
address = "United States",
}