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Molecular packing structure of fibrin fibers resolved by X-ray scattering and molecular modeling
AMOLF, Biol Soft Matter Grp, Utrecht, Netherlands.;UMC Utrecht, Dept Pathol, NL-3508 GA Utrecht, Netherlands..
KTH, School of Electrical Engineering and Computer Science (EECS), Centres, Centre for High Performance Computing, PDC. Sechenov Univ, Moscow 119991, Russia..
AMOLF, Biol Soft Matter Grp, Utrecht, Netherlands.;Univ Munster, Ctr Mol Biol Inflammat, Inst Cell Biol, Munster, Germany..ORCID iD: 0000-0002-4325-6298
Univ Groningen, Zernike Inst Adv Mat, Macromol Chem & New Polymer Mat, Nijenborgh 4, NL-9747 AG Groningen, Netherlands..
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2020 (English)In: Soft Matter, ISSN 1744-683X, E-ISSN 1744-6848, Vol. 16, no 35, p. 8272-8283Article in journal (Refereed) Published
Abstract [en]

Fibrin is the major extracellular component of blood clots and a proteinaceous hydrogel used as a versatile biomaterial. Fibrin forms branched networks built of laterally associated double-stranded protofibrils. This multiscale hierarchical structure is crucial for the extraordinary mechanical resilience of blood clots, yet the structural basis of clot mechanical properties remains largely unclear due, in part, to the unresolved molecular packing of fibrin fibers. Here the packing structure of fibrin fibers is quantitatively assessed by combining Small Angle X-ray Scattering (SAXS) measurements of fibrin reconstituted under a wide range of conditions with computational molecular modeling of fibrin protofibrils. The number, positions, and intensities of the Bragg peaks observed in the SAXS experiments were reproduced computationally based on the all-atom molecular structure of reconstructed fibrin protofibrils. Specifically, the model correctly predicts the intensities of the reflections of the 22.5 nm axial repeat, corresponding to the half-staggered longitudinal arrangement of fibrin molecules. In addition, the SAXS measurements showed that protofibrils within fibrin fibers have a partially ordered lateral arrangement with a characteristic transverse repeat distance of 13 nm, irrespective of the fiber thickness. These findings provide fundamental insights into the molecular structure of fibrin clots that underlies their biological and physical properties.

Place, publisher, year, edition, pages
Royal Society of Chemistry (RSC) , 2020. Vol. 16, no 35, p. 8272-8283
National Category
Chemical Sciences
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URN: urn:nbn:se:kth:diva-283157DOI: 10.1039/d0sm00916dISI: 000569505000015PubMedID: 32935715Scopus ID: 2-s2.0-85091055272OAI: oai:DiVA.org:kth-283157DiVA, id: diva2:1473326
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QC 20201006

Available from: 2020-10-06 Created: 2020-10-06 Last updated: 2022-06-25Bibliographically approved

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Zhmurov, Artem

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