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Combinatorial methods for discovery of peptide ligands which bind to antibody‐like molecules
Author(s) -
Tribbick Gordon,
Rodda Stuart
Publication year - 2002
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.592
Subject(s) - peptide , bence jones protein , chemistry , ligand (biochemistry) , computational biology , molecule , peptide library , combinatorial chemistry , antibody , peptide sequence , stereochemistry , biochemistry , biology , immunoglobulin light chain , immunology , receptor , organic chemistry , gene
In the 1980s, new methods of parallel peptide synthesis were used to make large libraries of peptides, which were then screened for binding to Bence–Jones dimers. Subsequent X‐ray crystallography of the Bence–Jones proteins, which had been infiltrated with peptide ligand, was used to determine the structural correlate of the binding data. The mode of binding was found to be not predictable and insight was gained into the forces determining how the so‐called mimotopes interacted with binding sites. Copyright © 2002 John Wiley & Sons, Ltd.