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...
Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1991. - 24(2008), 9 vom: 06. Mai, Seite 4979-88 |
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1. Verfasser: | |
Weitere Verfasser: | , , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2008
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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 |
Zusammenfassung: | 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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Beschreibung: | Date Completed 11.06.2008 Date Revised 29.04.2008 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 0743-7463 |
DOI: | 10.1021/la703264x |