QSAR of multiple mutated antibodies
✍ Scribed by Ilona Mandrika; Peteris Prusis; Sviatlana Yahorava; Kaspars Tars; Jarl E.S. Wikberg
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 193 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0952-3499
- DOI
- 10.1002/jmr.817
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✦ Synopsis
Abstract
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.
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