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240216s2024 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.3c03132
|2 doi
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|a eng
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|a Saha, Sanjib
|e verfasserin
|4 aut
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|a On the Mechanism of Self-Assembly of Fibrinogen in Thrombin-free Aqueous Solution
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|c 2024
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|a Text
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Revised 27.02.2024
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|a published: Print-Electronic
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|a Citation Status PubMed-not-MEDLINE
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|a 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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|a Journal Article
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|a Büngeler, Anne
|e verfasserin
|4 aut
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|a Hense, Dominik
|e verfasserin
|4 aut
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|a Strube, Oliver I
|e verfasserin
|4 aut
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| 700 |
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|a Huber, Klaus
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 40(2024), 8 vom: 27. Feb., Seite 4152-4163
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|g year:2024
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|g day:27
|g month:02
|g pages:4152-4163
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|u http://dx.doi.org/10.1021/acs.langmuir.3c03132
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