Folding a De Novo Designed Peptide into an α‐Helix through Hydrophobic Binding by a Bowl‐Shaped Host | Zendy

Tashiro Shohei | Zendy; Tominaga Masahide | Zendy; Yamaguchi Yoshiki | Zendy; Kato Koichi | Zendy; Fujita Makoto | Zendy

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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+).

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