title: Von Willlebrand adhesion to surfaces at high shear rates is controlled by long-lived bonds.
abstract: Von Willebrand factor (vWF) adsorbs and immobilizes platelets at sites of injury under high-shear-rate conditions. It has been recently demonstrated that single vWF molecules only adsorb significantly to collagen above a threshold shear, and here we explain such counterintuitive behavior using a coarse-grained simulation and a phenomenological theory. We find that shear-induced adsorption only occurs if the vWF-surface bonds are slip-resistant such that force-induced unbinding is suppressed, which occurs in many biological bonds (i.e., catch bonds). Our results quantitatively match experimental observations and may be important to understand the activation and mechanical regulation of vWF activity during blood clotting.
authors.affiliation: Department of Materials Science and Engineering, Northwestern University, Evanston, Illinois. Electronic address: cesing@mit.edu.
authors.forename: Charles E
authors.initials: CE
authors.lastname: Sing
authors.forename: Jennifer G
authors.initials: JG
authors.lastname: Selvidge
authors.forename: Alfredo
authors.initials: A
authors.lastname: Alexander-Katz
mesh_terms: D000327:Adsorption; D001696:Biomechanical Phenomena; D001792:Blood Platelets / Q000737:chemistry; D055595:Mechanical Phenomena; D008958:Models, Molecular; D013499:Surface Properties; D014841:von Willebrand Factor / Q000737:chemistry*
chemical_list: D014841:von Willebrand Factor
references.citation: Langmuir. 2011 Nov 15;27(22):13796-805
references.pmid: 21977962
references.citation: Biophys J. 2010 May 19;98(9):L35-7
references.pmid: 20441731
references.citation: Science. 2002 Aug 16;297(5584):1176-9
references.pmid: 12183630
references.citation: Nat Med. 2009 Jun;15(6):665-73
references.pmid: 19465929
references.citation: Phys Rev Lett. 2006 Sep 29;97(13):138101
references.pmid: 17026077
references.citation: Science. 1978 May 12;200(4342):618-27
references.pmid: 347575
references.citation: J Chem Phys. 2009 Dec 14;131(22):224902
references.pmid: 20001079
references.citation: J Biol Chem. 2003 Apr 25;278(17):15035-9
references.pmid: 12582178
references.citation: Nat Commun. 2013;4:1333
references.pmid: 23299883
references.citation: Blood. 1996 Oct 15;88(8):2939-50
references.pmid: 8874190
references.citation: Curr Opin Struct Biol. 2009 Feb;19(1):50-5
references.pmid: 19157853
references.citation: Annu Rev Biochem. 1998;67:395-424
references.pmid: 9759493
references.citation: Phys Rev Lett. 2003 Jul 18;91(3):038102
references.pmid: 12906459
references.citation: Science. 2009 Jun 5;324(5932):1330-4
references.pmid: 19498171
references.citation: J Thromb Haemost. 2011 Jul;9 Suppl 1:130-43
references.pmid: 21781248
references.citation: J Chem Phys. 2011 Jul 7;135(1):014902
references.pmid: 21744916
references.citation: Phys Rev Lett. 2006 Sep 29;97(13):138103
references.pmid: 17026079
references.citation: Thromb Haemost. 2007 Aug;98(2):283-6
references.pmid: 17721608
references.citation: Proc Natl Acad Sci U S A. 2007 May 8;104(19):7899-903
references.pmid: 17470810
references.citation: Nature. 2010 Aug 19;466(7309):992-5
references.pmid: 20725043
references.citation: Haemophilia. 2008 Nov;14 Suppl 5:11-26
references.pmid: 18786007
references.citation: J Thromb Haemost. 2004 Apr;2(4):561-73
references.pmid: 15102010