title: Peptides and Peptide Analogs to Inhibit Protein-Protein Interactions.
abstract: Protein-protein interactions are governed by relatively few amino acid residues at the binding interface. Peptides derived from these protein regions may serve as mimics of one of the interaction partners in structural studies or as inhibitors to disrupt the respective interaction and investigate its biological consequences. Inhibitory peptides may also be lead structures for drug development if the respective protein-protein interaction is essential for a pathogen or disease mechanism. Binding peptides may be systematically derived from one of the binding partners or found in the screen of combinatorial peptide libraries. Molecular modelling based on structural data helps to refine existing peptides or even design novel binding peptides. This chapter gives an outline of the binding peptide discovery process and subsequent chemical modifications to further enhance affinity and specificity and to increase stability against degradation in vivo. Examples from the past three decades illustrate the great diversity of applications for protein binding peptides and peptide analogs.
authors.affiliation: Technische Universität Darmstadt, Clemens-Schöpf-Institut für Organische Chemie und Biochemie, Alarich-Weiss-Straße 4, 64287, Darmstadt, Germany.
authors.forename: Dorothea
authors.initials: D
authors.lastname: Helmer
authors.affiliation: Technische Universität Darmstadt, Clemens-Schöpf-Institut für Organische Chemie und Biochemie, Alarich-Weiss-Straße 4, 64287, Darmstadt, Germany. schmitz@biochemie.tu-darmstadt.de.
authors.forename: Katja
authors.initials: K
authors.lastname: Schmitz
mesh_terms: D000818:Animals; D015195:Drug Design; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry* / Q000494:pharmacology*; D011485:Protein Binding; D060066:Protein Interaction Maps / Q000187:drug effects*
chemical_list: D010446:Peptide Fragments
keywords: Combinatorial libraries; Inhibitors; Peptide mimetics; Peptides; Protein-protein interactions; Rational design; Solid-phase peptide synthesis