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Drug platforms

Functionalizing mAbs with a noncovalent peptide-binding site

A peptide-binding site found on Erbitux cetuximab could be used to functionalize mAbs without disrupting their native antigen-binding properties. Crystal structure, biophysical and sequencing studies identified a unique site in the Fab framework of Erbitux that can noncovalently bind to an engineered peptide called a meditope. The binding site was grafted onto Herceptin trastuzumab. In HER2 (EGFR2; ErbB2; neu)+ human breast cancer cell lines, the modified trastuzumab bound with affinity comparable to that of unmodified trastuzumab and was also shown to bind with a meditope-Fc construct. Next steps include trying to improve the affinity of the meditope-mAb interaction and evaluating the use of meditope-enabled mAbs for research and therapeutic applications.
Meditope Biosciences Inc. is developing meditope-enabled mAbs and corresponding meditopes.
Roche's Genentech Inc. unit markets Herceptin, a humanized mAb against HER2, to treat breast and gastric cancers.
Eli Lilly and Co., Bristol-Myers Squibb Co. and Merck KGaA market Erbitux, a chimeric IgG1 mAb targeting epidermal growth factor receptor (EGFR), to treat colorectal cancer and head and neck cancer (see Building meditope-enabled mAbs, page 1).

SciBX 6(42); doi:10.1038/scibx.2013.1203
Published online Oct. 31, 2013

Patent applications filed by City of Hope; exclusively licensed to Meditope; available for partnering through Meditope

Donaldson, J.M. et al. Proc. Natl. Acad. Sci. USA; published online
Oct. 7, 2013;
Contact: John C. Williams, Beckman Research Institute at City of Hope, Duarte, Calif.