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Multi-parametric analysis reveals enhanced G2-phase arrest of an optimized anti-HER2 antibody to inhibit breast
Chunxia Qiao1, Xiaoling Lang2, Longlong Luo1
1Laboratory of Molecular Immunology, Institute of Basic Medical Sciences, P. O. Box 130 (3), Taiping Road #27 Haidian, Beijing, 100850, China.
Objectives:
To find a "me-better" antibody by epitope-specific antibody optimization and multi-parametric analysis.
Results:
Using epitope-specific library based on the commercial drug, Pertuzumab/2C4, we screened a novel human anti-HER2 antibody, MIL5, which has slightly higher affinity than the drug. MIL5 and 2C4 share the same epitope to bind HER2; however, MIL5 bound to HER2 His235-His245 more tightly than 2C4, which could be the main reason of its enhanced affinity. In vivo experiments also showed MIL5 had stronger anti-cancer activity than 2C4; however, the classical flow cytometry assays to detect cell apoptosis or cycling did not show convincing evidence of the advantages of MIL5. Thus we introduced the multi-parameter in-cell analysis method to evaluate the superiority of MIL5 to 2C4 in arresting cancer cells in G2-phase to inhibit cell growth and/or proliferation.
Conclusion:
Multi-parametric method confirmed stronger arrest of G2 by MIL5 to show better anti-cancer function both in vitro and in vivo than 2C4.
