Open AccessSpecificity Profiling of Protein‐Binding Domains Using One‐Bead‐One‐Compound Peptide Libraries
Author(s) -
Kunys Andrew R.,
Lian Wenlong,
Pei Dehua
Publication year - 2012
Publication title -
current protocols in chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.503
H-Index - 14
ISSN - 2160-4762
DOI - 10.1002/9780470559277.ch120125
Subject(s) - peptide library , peptide , chemistry , phage display , combinatorial chemistry , computational biology , biochemistry , pdz domain , template , covalent bond , peptide sequence , biology , nanotechnology , materials science , organic chemistry , gene
One‐bead‐one‐compound (OBOC) libraries consist of structurally related compounds (e.g., peptides) covalently attached to a solid support, with each resin bead carrying a unique compound. OBOC libraries of high structural diversity can be rapidly synthesized and screened without the need for any special equipment, and therefore can be employed in any chemical or biochemical laboratory. OBOC peptide libraries have been widely used to map the ligand specificity of proteins, to determine the substrate specificity of enzymes, and to develop inhibitors against macromolecular targets. They have proven particularly useful in profiling the binding specificity of protein modular domains (e.g., SH2 domains, BIR domains, and PDZ domains); subsequently, the specificity information can be used to predict the protein targets of these domains. The protocols outlined in this article describe the methodologies for synthesizing and screening OBOC peptide libraries against SH2 and PDZ domains, and the related data analysis. Curr. Protoc. Chem. Biol . 4:331‐355 © 2012 by John Wiley & Sons, Inc.