Peptides and Peptide Analogs to Inhibit Protein-Protein Interactions

被引:13
|
作者
Helmer, Dorothea [1 ]
Schmitz, Katja [1 ]
机构
[1] Tech Univ Darmstadt, Clemens Schopf Inst Organ Chem & Biochem, Alarich Weiss Str 4, D-64287 Darmstadt, Germany
关键词
Peptides; Inhibitors; Protein-protein interactions; Peptide mimetics; Solid-phase peptidesynthesis; Combinatorial libraries; Rational design; PARTIAL EDMAN DEGRADATION; COMBINATORIAL LIBRARY; GENERAL-METHOD; BINDING-SITE; IN-VIVO; INTERACTION NETWORKS; STRUCTURAL BASIS; PEPTOID HYBRIDS; LIGAND-BINDING; SPOT-SYNTHESIS;
D O I
10.1007/978-3-319-32805-8_8
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
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页码:147 / 183
页数:37
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