Affimed's fully human fab antibody AFM-14 predominantly binds to the activated form of a receptor (GPIIb/IIIa) that plays a major role in the formation of blood clots. The pre-clinical studies, conducted at the Dept. Cardiology and Dept. Clinical Pharmacology of Freiburg University, Germany and at the Baker Heart Research Institute in Melbourne, Australia demonstrated that the antithrombotic effect is comparable to the clinically used conformation-unspecific GPIIb/GPIIIa blockers tirofiban and eptifibatide. However, in clear contrast to these blockers, Affimed’s antibody did not prolong bleeding times. This antibody thus represents a novel future approach for antiplatelet therapy. The results of these studies were published in Circ Res. 2006; 99:25-33 [1].

"Our antibody for thrombosis offers very significant advantages over existing anti-thrombotic antibodies" commented Prof. Little, CSO of Affimed, "For a start our antibody is fully human, can be manufactured cost-effectively in E.coli and binds predominantly to the activated receptor in marked contrast to other antibody therapies for thrombosis"

The current antibody on the market for thrombosis is Reopro, a chimeric antibody that does not distinguish between the activated and non-activated forms of the GPIIb/IIIa receptor on blood platelets. Reopro is also produced first as a full length antibody in mammalian cells and enzymatically treated to release Fab fragments, which then have to be purified.

[1]Schwarz M, Meade G, Stoll P, Ylanne J, Bassler N, Chen YC, et al. Conformation-specific blockade of the integrin GPIIb/IIIa: A novel antiplatelet strategy that selectively targets activated platelets. Circ Res 2006;99:25-33.

International Patent Application PCT/EP02/11154 "Antibody of human origin for inhibiting thrombocyte aggregation" See also: "Single-chain antibodies for the conformation-specific blockade of activated platelet integrin alphaIIbeta3 designed by subtractive selection from naïve human phage libraries" by Schwarz et al. FASEB J. (2004) 18, 1704.

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