Protein Tomography™ Reveals Molecular Mode of Action of Humax-EGFr Published in PNAS
News Apr 23, 2008
Sidec AB announced that together with Genmab the molecular mode of action of HuMax-EGFr (zalutumumab) has been determined. It was shown that zalutumumab locks the epidermal growth factor receptor (EGFr) molecules into a compact, inactive conformation. Flexibility is crucial to the role of the EGFr in signaling, and this study, done with Sidec's proprietary methodology Protein Tomography(TM), has played a central role in the understanding of the inhibition of individual EGFr molecules.
Moreover, Sidec's unique technology confirmed that HuMax-EGFr binds bivalently to the EGFr. Prevention of the receptor dimerization as well as locking the EGFr molecules in the inactive form both contribute to the inhibition of signaling and cancer cell growth.
This data will be demonstrated on Sidec's First Protein Tomography Symposium at the fourth annual PEGS Summit 28 April - 2 May at the Intercontinental Hotel in Boston.
With Protein Tomography™ it is possible to study the molecular mode of action of individual molecules in situ and in vitro. The biological information obtained can also be used to prioritize the most promising monoclonal antibodies/projects and to locate the antibody binding epitope.
"These results clearly show the importance of understanding the molecular mode of action and to capture the flexibility of a receptor when developing therapeutic antibodies. Today this can only be done with Protein Tomography™ and we are proud to have contributed to Genmab's new insight to HuMax-EGFr mechanism of action." says Hans Johansson CEO at Sidec AB.
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