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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. This Article Full Text (PDF) Supplemental Tables and Figure All Versions of this Article: blood-2006-03-011965v1 108/12/3753    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Lisman, T. Articles by Farndale, R. W Search for Related Content PubMed PubMed Citation Articles by Lisman, T. Articles by Farndale, R. W Related Collections Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted March 24, 2006 Accepted July 24, 2006 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* Department of Clinical Chemistry and Haematology, University Medical Centre Utrecht, Netherlands Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom Department of Crystal and Structural Chemistry, Utrecht University, Utrecht, Netherlands * Corresponding author; email: rwf10{at}cam.ac.uk. The essential event in platelet adhesion to the injured blood vessel wall is the binding to sub-endothelial collagen of plasma von Willebrand factor (VWF), a protein which interacts transiently with platelet glycoprotein (GP) Ib1-3, slowing circulating platelets to facilitate firm adhesion through collagen receptors, including integrin 21 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 #23 alone bound VWF, with similar affinity to that of native collagen III. Immobilized peptide #23 supported platelet adhesion under static and flow conditions, processes blocked by an antibody which prevents collagen from binding the VWF A3 domain. Truncated and alanine-substituted peptides derived from #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. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: When collagen meets VWF Hans Deckmyn and Karen Vanhoorelbeke Blood 2006 108: 3628. [Full Text] [PDF] This article has been cited by other articles: A. B. Herr and R. W. Farndale Structural Insights into the Interactions between Platelet Receptors and Fibrillar Collagen J. Biol. Chem., July 24, 2009; 284(30): 19781 - 19785. [Abstract] [Full Text] [PDF] E. Hohenester, T. Sasaki, C. Giudici, R. W. Farndale, and H. P. Bachinger Structural basis of sequence-specific collagen recognition by SPARC PNAS, November 25, 2008; 105(47): 18273 - 18277. [Abstract] [Full Text] [PDF] S. M. Sweeney, J. P. Orgel, A. Fertala, J. D. McAuliffe, K. R. Turner, G. A. Di Lullo, S. Chen, O. Antipova, S. Perumal, L. Ala-Kokko, et al. 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