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

Angewandte Chemie - International Edition

Volumn 49, Issue 39, 2010, Pages 7111-7115

  Zaminer, Jan ^a   Brockmann, Christoph ^b   Huy, Peter ^a   Opitz, Robert ^b   Reuter, Cédric ^a   Beyermann, Michael ^b   Freund, Christian ^b   Müller, Matthias ^b   Oschkinat, Hartmut ^b   Schmalz, Hans Günther ^a   Kühne, Ronald ^b  

^a UNIVERSITY OF COLOGNE   (Germany)

^b LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

Author keywords

Conformational analysis; Molecular modeling; Peptide mimics; Protein protein interactions; Ring closing metathesis

Indexed keywords

BINDING ABILITIES; BINDING LIGANDS; CONFORMATIONAL ANALYSIS; DIPEPTIDE; DOUBLE BONDS; HELIX CONFORMATION; PEPTIDE MIMICS; POLYPROLINE; PROLINE-RICH MOTIF; PROTEIN-PROTEIN INTERACTIONS; RING CLOSING METATHESIS; SMALL MOLECULES; STEREO-SELECTIVE; TYPE II;

AMINO ACIDS; CHELATION; MOLECULAR MODELING; ORGANIC ACIDS; PEPTIDES; SYNTHESIS (CHEMICAL);

CONFORMATIONS;

DIPEPTIDE; LIGAND; PEPTIDE; PROLYL-PROLINE; PROLYLPROLINE;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROLINE RICH PROTEIN DOMAIN; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STEREOISOMERISM; SYNTHESIS;

AMINO ACID SEQUENCE; DIPEPTIDES; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES; PROLINE-RICH PROTEIN DOMAINS; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STEREOISOMERISM;

EID: 77956943226     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201001739     Document Type: Article

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