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 | Zendy

Zaminer Jan | Zendy; Brockmann Christoph | Zendy; Huy Peter | Zendy; Opitz Robert | Zendy; Reuter Cédric | Zendy; Beyermann Michael | Zendy; Freund Christian | Zendy; Müller Matthias | Zendy; Oschkinat Hartmut | Zendy; Kühne Ronald | Zendy; Schmalz HansGünther | Zendy

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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.

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