Complexity of "A-a" knob-hole fibrin interaction revealed by atomic force spectroscopy

During blood vessel injury, fibrinogen is converted to fibrin, a polymer that serves as the structural scaffold of a blood clot. The primary function of fibrin is to withstand the large shear forces in blood and provide mechanical stability to the clot, protecting the wound. Understanding the biophy...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1991. - 24(2008), 9 vom: 06. Mai, Seite 4979-88
1. Verfasser: Averett, Laurel E (VerfasserIn)
Weitere Verfasser: Geer, Carri B, Fuierer, Ryan R, Akhremitchev, Boris B, Gorkun, Oleg V, Schoenfisch, Mark H
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2008
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Fibrin 9001-31-4
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245 1 0 |a Complexity of "A-a" knob-hole fibrin interaction revealed by atomic force spectroscopy 
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520 |a During blood vessel injury, fibrinogen is converted to fibrin, a polymer that serves as the structural scaffold of a blood clot. The primary function of fibrin is to withstand the large shear forces in blood and provide mechanical stability to the clot, protecting the wound. Understanding the biophysical forces involved in maintaining fibrin structure is of great interest to the biomedical community. Previous reports have identified the "A-a" knob-hole interaction as the dominant force responsible for fibrin's structural integrity. Herein, biochemical force spectroscopy is used to study knob-hole interactions between fibrin fragments and variant fibrinogen molecules to identify the forces occurring between individual fibrin molecules. The rupture of the "A-a" knob-hole interaction results in a characteristic profile previously unreported in fibrin force spectroscopy with two distinct populations of specific forces: 110 +/- 34 and 224 +/- 31 pN. In the absence of a functional "A" knob or hole "a", these forces cease to exist. We propose that the characteristic pattern represents the deformation of the D region of fibrinogen prior to the rupture of the "A-a" knob-hole bond 
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650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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700 1 |a Geer, Carri B  |e verfasserin  |4 aut 
700 1 |a Fuierer, Ryan R  |e verfasserin  |4 aut 
700 1 |a Akhremitchev, Boris B  |e verfasserin  |4 aut 
700 1 |a Gorkun, Oleg V  |e verfasserin  |4 aut 
700 1 |a Schoenfisch, Mark H  |e verfasserin  |4 aut 
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