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Addressing Protein–Protein Interactions with Small Molecules: A Pro‐Pro Dipeptide Mimic with a PPII Helix Conformation as a Module for the Synthesis of PRD‐Binding Ligands
Author(s) -
Zaminer Jan,
Brockmann Christoph,
Huy Peter,
Opitz Robert,
Reuter Cédric,
Beyermann Michael,
Freund Christian,
Müller Matthias,
Oschkinat Hartmut,
Kühne Ronald,
Schmalz HansGünther
Publication year - 2010
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.201001739
Subject(s) - polyproline helix , dipeptide , chemistry , stereochemistry , small molecule , helix (gastropod) , proline , amino acid , peptide , biochemistry , biology , ecology , snail
X marks the spot : The synthetic tricyclic amino acid X (see structure; C gray, H cyan, N blue, O red, double bond yellow) can be incorporated, without loss of binding ability, as a Pro‐Pro substitute into two peptides that bind to the proline‐rich motif‐recognizing domains Fyn‐SH3. The dipeptide analogue X , which is locked in a polyproline type II helix conformation, is created by stereoselective introduction of a vinylidene bridge into a diproline unit.