On the Mechanism of Self-Assembly of Fibrinogen in Thrombin-free Aqueous Solution
Fibrinogen dissolved in 0.12 M aqueous NaCl solution at a pH of 6.6 exhibits self-assembly in response to a lowering of the NaCl concentration to values equal to or lower than 60 mM. As has been established in a preceding work (Langmuir 2019, 35, and 12113), a characteristic signature of the self-as...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 40(2024), 8 vom: 27. Feb., Seite 4152-4163 |
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| Weitere Verfasser: | , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2024
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article |
| Zusammenfassung: | Fibrinogen dissolved in 0.12 M aqueous NaCl solution at a pH of 6.6 exhibits self-assembly in response to a lowering of the NaCl concentration to values equal to or lower than 60 mM. As has been established in a preceding work (Langmuir 2019, 35, and 12113), a characteristic signature of the self-assembly triggered by a drop in ionic strength is the formation of large globular particles. Growth of these particles most likely obeys a coalescence-like process also termed a step growth process. In order to extend this knowledge, the present work first optimized the protocol, leading to highly reproducible self-assembly experiments. Based on this optimization, the work succeeded in identifying an initial stage, not yet accessible, during which rigid short fibrils grow in close analogy to the thrombin-catalyzed polymerization of fibrin. In addition, first suggestions could be made on the transformation of these fibrils into larger aggregates, which upon drying turn into thick fiber-like ropes |
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| Beschreibung: | Date Revised 27.02.2024 published: Print-Electronic Citation Status PubMed-not-MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.3c03132 |