Contemporary strategies for the stabilization of peptides in the α-helical conformation

Laura K. Henchey, Andrea L. Jochim, Paramjit S. Arora

Research output: Contribution to journalReview articlepeer-review


Herein we review contemporary synthetic and protein design strategies to stabilize the α-helical motif in short peptides and miniature proteins. Advances in organometallic catalyst design, specifically for the olefin metathesis reaction, enable the use of hydrocarbon bridges to either crosslink side chains of specific residues or mimic intramolecular hydrogen bonds with carbon-carbon bonds. The resulting hydrocarbon-stapled and hydrogen bond surrogate α-helices provide unique synthetic ligands for targeting biomolecules. In the protein design realm, several classes of miniature proteins that display stable helical domains have been engineered and manipulated with powerful in vitro selection technologies to yield libraries of sequences that retain their helical folds. Rational re-design of these scaffolds provide distinctive reagents for the modulation of protein-protein interactions.

Original languageEnglish (US)
Pages (from-to)692-697
Number of pages6
JournalCurrent Opinion in Chemical Biology
Issue number6
StatePublished - Dec 2008

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry


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