The Study of changes in affinity of Anti-CD۲۰ antibody with mutations Tyr۱۰۱ and Tyr۱۰۷ to Arg in CDR۳ using docking

Backgrounds: CD۲۰ as the first general B-cell marker is expressed on the surface of all late pre-B lymphocytes. Antibodies which now serve as the first line of therapy for certain cancer fordiagnosis and treatment of cancer, have proven their value. Rituximab which is a chimeric mAbAnti-CD۲۰ triggers cell death by binding to CD۲۰ protein. Recently, using molecular simulationand modeling, designed a novel recombinant chimeric antibody and anticipated binding thisantibody to epitope by molecular docking.Materials and Methods: In this study, a potent AntiCD۲۰ antibody that had seen selected usingthe PDB site, were used for designing mutation in CDR۳ and docking. Since the CDR۳ domainplays an important role in binding antibodies to the epitope, Tyr ۱۰۱ and ۱۰۷ were mutated toArg in the CDR۳ domain. HADDOCK software structural prediction of the antibody-CD۲۰complex was used for designing and validation of CDR۳of antibodies with higher affinity forbinding to CD۲۰ receptor.Results: The data obtained from HADDOCK, including Z-Score and bond energy, wereanalyzed which were -۱.۴ and -۲۸.۵ in the native state and -۱.۹ and -۴۰.۹ in the moment state,respectively.Conclusion: Calictibly by analyzing and comparing the data obtained from HADDOCK,between normal and mutant modes, it was found that by creating this mutation in CDR۳ ofantibody, increased binding affinity to antigen and their properties improved predictably for theirbinding ability to CD۲۰.

کلیدواژه ها:

Anti-CD۲۰ Antibody ، CDR۳ ، Site-directed Mutation