Improvement of the multi-specificity for anti-IDH1/2 mAb MsMab-1 and 2 based on structure

2015 Fiscal Year Final Research Report

• Project/Area Number: 26840015
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry
• Research Institution: Tohoku University
• Principal Investigator: Ogasawara Satoshi 東北大学, 医学(系)研究科(研究院), 助教 (30546685)
• Project Period (FY): 2014-04-01 – 2016-03-31
• Keywords: モノクローナル抗体 / 多重特異性 / X線結晶構造解析

Outline of Final Research Achievements

We tried to solve the crystal structure of MsMab-1 and 2. We identified a critical amino acid residue for the multi-specificity from the crystal structure of MsMab-1. Hence MsMab-1 was mutated the amino acid residue of antigen recognition site based on the structure. Mutated MsMab-1 was changed the specificity against mutated IDH1/2. MsMab-2 was not able to try a crystallization experiment for its low level of productivity.
We generated a novel multi-specific anti-IDH1/2 monoclonal antibody MsMab-3, which could bind mutated IDH1/2 peptides but not mutated IDH1/2 proteins.

Free Research Field

構造生物化学