Thursday, October 31, 2013
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Functionalizing mAbs with a
noncovalent peptide-binding site
A peptide-binding site
found on Erbitux
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
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.
Biosciences Inc. is developing meditope-enabled mAbs and
Inc. unit markets Herceptin, a humanized mAb against HER2,
to treat breast and gastric cancers.
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).
Published online Oct. 31, 2013
Patent applications filed
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.
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