Single turn peptide alpha helices with exceptional stability in water.
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.
Shepherd
Nicholas E
NE
Centre for Drug Design and Development, Institute for Molecular Bioscience, University of Queensland, Brisbane, Qld 4072, Australia.
Hoang
Huy N
HN
Abbenante
Giovanni
G
Fairlie
David P
DP
D002942:Circular Dichroism; D004355:Drug Stability; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000737:chemistry / Q000378:metabolism; D010456:Peptides, Cyclic / Q000737:chemistry*; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D012997:Solvents; D013696:Temperature; D014867:Water / Q000737:chemistry*
D009842:Oligopeptides; D010456:Peptides, Cyclic; D012997:Solvents; D014867:Water; D010447:Peptide Hydrolases