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| home > ebr > spring 2003 > spr analysis of rationally designed anti-her2 exocyclic mimetics of antibodies |
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European BioPharmaceutical Review
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| A series of peptide mimetics, based on the structure of the CDR3 loop of the anti-HER2 mAb 4D5, an anti-oncoprotein therapeutic monoclonal antibody, have been designed. The peptides can disable the tyrosine kinase, p185HER2/neu (HER2), an oncoprotein commonly expressed in human breast, ovarian and colon cancers. In SPR studies, the peptides have been shown to directly bind to HER2 and to compete with mAb 4D5 for receptor binding. Dissociation rate constants were shown to be important determinants of anti-tumorigenic activity of the peptides. |
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By Dr Ramachandran Murali, Assistant Professor in the Department of Pathology and Laboratory of Medicine at the University of Pennsylvania, USA
Dr Ramachandran Murali
Dr Ramachandran Murali is Assistant Professor in the Department of Pathology and Laboratory of Medicine, University of Pennsylvania School of Medicine. He is also a visiting academic at the Sir William Dunn School of Pathology, Oxford University, UK and a well trained and established structural biologist. He obtained his doctoral degree in Biophysics from the University of Madras, India, one of the pioneering institutes for structural biology in India.
Since then Dr Murali has expanded his expertise in macromolecular crystallography, immunology and cancer biology. His laboratory is mainly interested in the structure and function aspects of cell surface receptors relevant for cancer biology and immunology. His contributions include antibody structures, small molecule modifiers of receptors which have therapeutic applications in cancer biology, and autoimmune pathologies. He has developed several therapeutically relevant small molecules in the Department of Pathology and Laboratory Medicine, Center for Receptor Biology and Cell Growth at the University of Pennsylvania School of Medicine.
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