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Blood, 1 December 2006, Vol. 108, No. 12, pp. 3753-3756.
Prepublished online as a Blood First Edition Paper on August 15, 2006; DOI 10.1182/blood-2006-03-011965.
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HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Brief report
A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptides
Ton Lisman,
Nicolas Raynal,
Dafna Groeneveld,
Ben Maddox,
Anthony R. Peachey,
Eric G. Huizinga,
Philip G. de Groot, and
Richard W. Farndale
From the Department of Clinical Chemistry and Haematology, University Medical Centre Utrecht, The Netherlands; the Department of Biochemistry, University of Cambridge, United Kingdom; and the Department of Crystal and Structural Chemistry, Utrecht University, The Netherlands.
The essential event in platelet adhesion to the injured blood vessel wall is the binding to subendothelial collagen of plasma von Willebrand factor (VWF), a protein that interacts transiently with platelet glycoprotein Ib (GPIb), slowing circulating platelets to facilitate firm adhesion through collagen receptors, including integrin 2 1 and GpVI. To locate the site in collagen that binds VWF, we synthesized 57 overlapping triple-helical peptides comprising the whole triple-helical domain of collagen III. Peptide no. 23 alone bound VWF, with similar affinity to that of native collagen III. Immobilized peptide no. 23 supported platelet adhesion under static and flow conditions, processes blocked by an antibody that prevents collagen from binding the VWF A3 domain. Truncated and alanine-substituted peptides derived from no. 23 either strongly interacted with both VWF and platelets or lacked both VWF and platelet binding. Thus, we identified the sequence RGQOGVMGF (O is hydroxyproline) as the minimal VWF-binding sequence in collagen III.
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