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QSAR of multiple mutated antibodies
Author(s) -
Mandrika Ilona,
Prusis Peteris,
Yahorava Sviatlana,
Tars Kaspars,
Wikberg Jarl E.S.
Publication year - 2007
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.817
Subject(s) - quantitative structure–activity relationship , monoclonal antibody , antibody , chemistry , mutagenesis , peptide , computational biology , antigen , combinatorial chemistry , stereochemistry , molecular model , biochemistry , biology , mutation , immunology , gene
The aim of this study was to develop predictive quantitative structure–activity relationship (QSAR) modeling for antibody‐peptide interactions. A small single chain antibody library was designed and manufactured around the murine anti‐p24 (HIV‐1) monoclonal antibody CB4‐1 by use of statistical molecular design (SMD) principles and site directed mutagenesis, and its affinity for a p24 derived antigen was determined by fluorescence polarization. A satisfactory QSAR model ( Q 2 = 0.74, R 2 = 0.88) was derived by correlating the affinity data to physicochemical property scales of the amino acids varied in the library. The model explains most of the antibody–antigen interactions of the studied set, and provides insights into the molecular mechanism involved in antigen binding. Copyright © 2007 John Wiley & Sons, Ltd.