Control of helix sense in protein-mimicking backbone by the noncovalent chiral effect.
We have reviewed our previous work regarding induction or control of a peptide helix sense through chiral stimulus to the peptide chain terminus. An optically inactive 3(10)-helix designed mainly with unusual alpha-amino acid residues was commonly employed. Such an N-terminal-free peptide generates a preferred helix sense by chiral acid molecule. A helix sense pre-directed in chiral sequence is also influenced or controlled by the chiral sign of such external molecule. Here free amide groups in the 3(10)-helical N-terminus participate in the formation of a multipoint coordinated complex. The terminal asymmetry produces the noncovalent chiral domino effect (NCDE) to influence the whole helix sense. The NCDE-mediated control of helicity provides the underlying chiral nature of protein-mimicking helical backbones: notably, chiral recognition at the terminus and modulation of helical propensity through chiral stimulus. The above items from our previous reports have been outlined and reviewed together with their significance in biopolymer science and chiral chemistry.
Inai
Yoshihito
Y
Department of Environmental Technology and Urban Planning; Shikumi College, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya 466-8555, Japan. inai.yoshihito@nitech.ac.jp
Komori
Hisatoshi
H
Ousaka
Naoki
N
D000596:Amino Acids / Q000737:chemistry; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013237:Stereoisomerism
D000596:Amino Acids; D010455:Peptides; D011506:Proteins