Conformational modulation of peptide secondary structures using β-aminobenzenesulfonic acid.
This communication describes the influence of β-aminobenzenesulfonic acid ((S)Ant) on the conformational preferences of hetero foldamers. The designed (Aib-(S)Ant-Aib)n and (Aib-(S)Ant-Pro)n oligomers display a well-defined folded conformation featuring intramolecular mixed hydrogen bonding (7/11) and intra-residual (6/5) H-bonding interactions, respectively.
Division of Organic Chemistry, National Chemical Laboratory, Homi Bhabha Road, Pune 411 008, India. gj.sanjayan@ncl.res.in.
Sangram S
SS
Kale
Shrikant M
SM
Kunjir
Rupesh L
RL
Gawade
Vedavati G
VG
Puranik
P R
PR
Rajamohanan
Gangadhar J
GJ
Sanjayan
D006860:Hydrogen Bonding; D009842:Oligopeptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013425:Sulfanilic Acids / Q000737:chemistry*
D009842:Oligopeptides; D013425:Sulfanilic Acids; C100048:2-sulfanilic acid