Abstract
Fibrin, the structural scaffold of blood clots, spontaneously polymerizes through the formation of 'A-a' knob-hole bonds. When subjected to external force, the dissociation of this bond is accompanied by two to four abrupt changes in molecular dimension observable as rupture events in a force curve. Herein, the configuration, molecular extension, and kinetic parameters of each rupture event are examined. The increases in contour length indicate that the D region of fibrinogen can lengthen by approximately 50% of the length of a fibrin monomer before rupture of the 'A-a' interaction. The dependence of the dissociation rate on applied force was obtained using probability distributions of rupture forces collected at different pull-off velocities. These distributions were fit using a model in which the effects of the shape of the binding potential are used to quantify the kinetic parameters of forced dissociation. We found that the weak initial rupture (i.e., event 1) was not well approximated by these models. The ruptured bonds comprising the strongest ruptures, events 2 and 3, had kinetic parameters similar to those commonly found for the mechanical unfolding of globular proteins. The bonds ruptured in event 4 were well described...Continue Reading
References
May 12, 1978·Science·G I Bell
Sep 1, 1982·Biopolymers·F J Roska, J D Ferry
Sep 1, 1982·Biopolymers·F J RoskaJ W Anderegg
Apr 1, 1997·Biophysical Journal·E Evans, K Ritchie
May 16, 1997·Science·M RiefH E Gaub
Dec 31, 1997·The Journal of Biological Chemistry·N OkumuraS T Lord
Dec 20, 2000·Proceedings of the National Academy of Sciences of the United States of America·Z YangR F Doolittle
Dec 2, 2004·Biophysical Chemistry·John W Weisel
Apr 20, 2005·Advances in Protein Chemistry·John W Weisel
Jul 7, 2005·Blood·Rustem I LitvinovJohn W Weisel
Nov 23, 2005·Biochemistry·Kenyon M Evans-NguyenMark H Schoenfisch
Jul 1, 1952·Proceedings of the National Academy of Sciences of the United States of America·J D Ferry
Apr 12, 2006·Physical Review Letters·Olga K DudkoAttila Szabo
May 13, 2006·Journal of Thrombosis and Haemostasis : JTH·N LaurensM P M de Maat
Dec 6, 2006·Biochemistry·Oleg V GorkunJohn W Weisel
Dec 19, 2006·Biophysical Journal·André E X BrownJohn W Weisel
Feb 8, 2007·The Journal of Physical Chemistry. B·Chad RayBoris B Akhremitchev
May 23, 2007·Proceedings of the National Academy of Sciences of the United States of America·Deepak SharmaHongbin Li
Oct 10, 2007·Journal of Thrombosis and Haemostasis : JTH·J W Weisel
Oct 24, 2007·Cell Biochemistry and Biophysics·M GutholdS T Lord
Feb 7, 2008·The Journal of Physical Chemistry. B·Robert B BestOlga K Dudko
Feb 26, 2008·Structure·Bernard B C LimKlaus Schulten
Mar 21, 2008·Langmuir : the ACS Journal of Surfaces and Colloids·Laurel E AverettMark H Schoenfisch
Jul 16, 2008·Biophysical Journal·Senli GuoBoris B Akhremitchev
Sep 3, 2008·Journal of Thrombosis and Haemostasis : JTH·M R FalvoS T Lord
Sep 20, 2008·Journal of the Royal Society, Interface·Paul A JanmeyJohn W Weisel
Oct 15, 2008·Proceedings of the National Academy of Sciences of the United States of America·Olga K DudkoAttila Szabo
Apr 23, 2009·Biophysical Journal·Senli GuoBoris B Akhremitchev
Citations
Oct 5, 2010·Biophysical Chemistry·Michael R FalvoSusan T Lord
Dec 17, 2014·Ukrainskiĭ biokhimicheskiĭ zhurnal·T A PozniakS V Komisarenko
Nov 4, 2010·Biophysical Journal·John R HouserMichael R Falvo
Nov 15, 2011·Structure·Artem ZhmurovValeri Barsegov
Aug 25, 2016·Progress in Biophysics and Molecular Biology·Douglas B Kell, Etheresia Pretorius
Feb 7, 2017·Journal of Thrombosis and Haemostasis : JTH·I K PiechockaG H Koenderink
May 22, 2018·Nanoscale·G Portale, J Torbet
Jun 5, 2015·PloS One·Caroline W WangMichael B Lawrence
May 26, 2010·The Analyst·Laurel E Averett, Mark H Schoenfisch
Jul 17, 2012·Journal of Cell Science·Pere Roca-CusachsMichael P Sheetz
May 26, 2010·Langmuir : the ACS Journal of Surfaces and Colloids·Chad RayBoris B Akhremitchev
Aug 25, 2010·Langmuir : the ACS Journal of Surfaces and Colloids·Laurel E AverettOleg V Gorkun