Relationship between salt-bridge identity and 14-helix stability of beta3-peptides in aqueous buffer.
We report a systematic analysis of the relationship between salt bridge composition and 14-helix structure within a family of model beta-peptides in aqueous buffer. We find an inverse relationship between side-chain length and the extent of 14-helix structure as judged by CD. Introduction of a stabilizing salt bridge pair within a previously reported beta-peptide ligand for hDM2 led to changes in structure that were detectable by NMR.
Department of Chemistry, Yale University, New Haven, Connecticut 06520, USA.
Danielle A
DA
Guarracino
Hyojin R
HR
Chiang
Tereece N
TN
Banks
James D
JD
Lear
Michael E
ME
Hodsdon
Alanna
A
Schepartz
D002021:Buffers; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D014867:Water / Q000737:chemistry
D002021:Buffers; D010455:Peptides; D014867:Water