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De Novo Protein Surface Design: Use of Cation–π Interactions to Enhance Binding between an α ‐Helical Peptide and a Cationic Molecule in 50 % Aqueous Solution
Author(s) -
Orner Brendan P.,
Salvatella Xavier,
Sánchez Quesada Jorge,
de Mendoza Javier,
Giralt Ernest,
Hamilton Andrew D.
Publication year - 2002
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 - 10.1002/1521-3773(20020104)41:1<117::aid-anie117>3.0.co;2-j
Subject(s) - cationic polymerization , peptide , chemistry , schematic , molecule , aqueous solution , hydrogen bond , nuclear magnetic resonance spectroscopy , stereochemistry , crystallography , combinatorial chemistry , biochemistry , polymer chemistry , organic chemistry , electronic engineering , engineering
The relative position of the Asp and Trp residues in a peptide chain is important for recognizing a tetraguanidinium receptor through hydrogen bonding and cation–π interactions. The molecule not only binds with high affinity ( K a =1.1×10 8 M −1 ), it also stabilizes the helical conformation of the peptide (see schematic representation) as demonstrated by NMR and CD spectroscopy.