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Protein Tomography(TM) Reveals Molecular Mode of Action of Humax-EGFr Published in PNAS
Date:4/22/2008

STOCKHOLM, April 22 /PRNewswire/ --

- Summary: Using Protein Tomography(TM), Sidec Investigated in Collaboration With Genmab the Molecular Mode of Action of Humax- EGFr (Zalutumumab). In This Study Sidec Showed That EGFr is Flexible and That Zalutumumab Locks the EGFr Into a Very Compact Inactive Conformation Thereby Inhibiting Cell Signaling and Cancer Cell Growth.

Sidec AB announced today 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.

(Logo: http://www.newscom.com/cgi-bin/prnh/20080220/294289 )

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 unique 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 Tomograph
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SOURCE Sidec AB
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