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Remarkable Stabilization of the α‐Helix Structure by an Intramolecular Host‐Guest Bridge in a Cyclodextrin‐Peptide Hybrid
Author(s) -
Hamasaki Keita,
Suzuki Ryosuke,
Mihara Hisakazu,
Ueno Akihiko
Publication year - 2001
Publication title -
macromolecular rapid communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.348
H-Index - 154
eISSN - 1521-3927
pISSN - 1022-1336
DOI - 10.1002/1521-3927(20010201)22:4<262::aid-marc262>3.0.co;2-o
Subject(s) - intramolecular force , peptide , cyclodextrin , chemistry , cholic acid , helix (gastropod) , stereochemistry , circular dichroism , salt bridge , biochemistry , bile acid , biology , ecology , snail , gene , mutant
A cyclodextrin‐peptide hybrid (CD‐peptide) bearing three units of γ‐cyclodextrin, cholic acid, and a dansyl fluorophore in the side chain has been prepared. In this novel CD‐peptide, the cholic acid unit acts as an internal guest and forms an intramolecular inclusion complex with γ‐cyclodextrin in the CD‐peptide. This intramolecular complex works as a host‐guest bridge in the CD‐peptide and remarkably stabilizes the α‐helix structure of the CD‐peptide.