This review covers chemical strategies for stabilizing peptide alpha-helices — stapling, hydrogen bond surrogates, side-chain crosslinks — that make helical peptide drugs stable and functional for clinical development.
Key findingContemporary helix stabilization strategies include hydrocarbon stapling, hydrogen bond surrogates, salt bridges, disulfide crosslinks, and unnatural
What the researchers found
Contemporary helix stabilization strategies include hydrocarbon stapling, hydrogen bond surrogates, salt bridges, disulfide crosslinks, and unnatural amino acids — chemical approaches that lock therapeutic peptides into bioactive helical conformations for clinical development.
Why it matters
Relevant for cyclic-peptides, peptide-design.
How the study worked
review study.
What this study cannot tell us
See abstract.
How to read the evidence
moderate evidence.
When this study was published
Published in 2008.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
Contemporary strategies for the stabilization of peptides in the alpha-helical conformation.
Current opinion in chemical biology, 12(6), 692-7
Citation
Henchey, Laura K; Jochim, Andrea L; Arora, Paramjit S. (2008). Contemporary strategies for the stabilization of peptides in the alpha-helical conformation.. Current opinion in chemical biology, 12(6), 692-7. https://doi.org/10.1016/j.cbpa.2008.08.019