QSAR of multiple mutated antibodies
2007 (English)In: Journal of Molecular Recognition, ISSN 0952-3499, E-ISSN 1099-1352, Vol. 20, no 2, 97-102 p.Article in journal (Refereed) Published
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 (Q2 = 0.74, R2 = 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.
Place, publisher, year, edition, pages
2007. Vol. 20, no 2, 97-102 p.
Amino acid physicochemical properties, Antibody library, Interaction site mapping, Peptide epitope, QSAR, Single chain antibody, Site directed mutagenesis, Statistical molecular design
IdentifiersURN: urn:nbn:se:uu:diva-15889DOI: 10.1002/jmr.817ISI: 000246169000004PubMedID: 17421049OAI: oai:DiVA.org:uu-15889DiVA: diva2:43660