Single turn peptide alpha helices with exceptional stability in water

Nicholas E Shepherd; Huy N Hoang; Giovanni Abbenante; David P Fairlie

doi:10.1021/ja0456003

Single turn peptide alpha helices with exceptional stability in water

J Am Chem Soc. 2005 Mar 9;127(9):2974-83. doi: 10.1021/ja0456003.

Authors

Nicholas E Shepherd¹, Huy N Hoang, Giovanni Abbenante, David P Fairlie

Affiliation

¹ Centre for Drug Design and Development, Institute for Molecular Bioscience, University of Queensland, Brisbane, Qld 4072, Australia.

PMID: 15740134
DOI: 10.1021/ja0456003

Abstract

Cyclic pentapeptides are not known to exist in alpha-helical conformations. CD and NMR spectra show that specific 20-membered cyclic pentapeptides, Ac-(cyclo-1,5) [KxxxD]-NH(2) and Ac-(cyclo-2,6)-R[KxxxD]-NH(2), are highly alpha-helical structures in water and independent of concentration, TFE, denaturants, and proteases. These are the smallest alpha-helical peptides in water.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Circular Dichroism
Drug Stability
Humans
Hydrogen Bonding
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Oligopeptides / chemistry*
Peptide Hydrolases / chemistry
Peptide Hydrolases / metabolism
Peptides, Cyclic / chemistry*
Protein Denaturation
Protein Structure, Secondary
Solvents
Temperature
Water / chemistry*

Substances

Oligopeptides
Peptides, Cyclic
Solvents
Water
Peptide Hydrolases