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Folding a De Novo Designed Peptide into an α‐Helix through Hydrophobic Binding by a Bowl‐Shaped Host
Author(s) -
Tashiro Shohei,
Tominaga Masahide,
Yamaguchi Yoshiki,
Kato Koichi,
Fujita Makoto
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200502802
Subject(s) - peptide , twist , chemistry , folding (dsp implementation) , host (biology) , residue (chemistry) , stereochemistry , crystallography , biophysics , biochemistry , biology , ecology , geometry , mathematics , electrical engineering , engineering
In a twist : Encapsulation of a nine‐residue peptide (Trp‐Ala‐Glu‐Ala‐Ala‐Ala‐Glu‐Ala‐Trp) within a bowl‐shaped coordination host in water induces and stabilizes the α‐helical conformation. The α‐helical peptide is recognized through two types of host–guest interactions: a hydrophobic interaction with both terminal Trp residues and electrostatic interactions between the Glu residues and the high positive charge of the host (12+).