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Helical sulfono-γ-AApeptides with predictable functions in protein recognition.

Peng SangYan ShiLulu WeiJianfeng Cai
Published in: RSC chemical biology (2022)
Sulfono-γ-AApeptides are a subset of possible sequence-specific foldamers that might be considered for the design of biomimetic drug molecular structures. Although they have been studied for a relatively short period of time, a number of structures and functions have been designed or discovered within this class of unnatural peptides. Examples of utilizing these sulfono-γ-AApeptides have demonstrated the potential that sulfono-γ-AApeptides can offer, however, to date, their application in biomedical sciences yet remains unexplored. This review mainly summarizes the helical folding conformations of sulfono-γ-AApeptides and their biological application as helical mimetics in medicinally relevant protein-protein interactions (PPIs) and assesses their potential for the mimicry of other α-helices for protein recognition in the future.
Keyphrases
  • amino acid
  • high resolution
  • protein protein
  • binding protein
  • human health
  • emergency department
  • small molecule
  • current status
  • adverse drug
  • drug induced
  • tissue engineering