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Spatial structure of fibrinopeptide B in water solution with DPC micelles by NMR spectroscopy
Institute of Physics, Kazan (Volga Region) Federal University.
Chemistry Institute, Kazan Federal University.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0002-6810-1882
Alexander Butlerov Institute of Chemistry, Kazan Federal University, Chemistry Institute, Kazan Federal University.
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2015 (English)In: Journal of Molecular Structure, ISSN 0022-2860, E-ISSN 1872-8014, Vol. 1102, p. 91-94Article in journal (Refereed) Published
Abstract [en]

Fibrinopeptide B (GluFib) is one of the factors of thrombosis. Normal blood protein soluble, fibrinogen (fibrinopeptide A and fibrinopeptide B), is transformed into the insoluble, fibrin, which in the form of filaments adheres to the vessel wall at the site of injury, forming a grid. However, the spatial structure of this peptide has not been established till now. In this article, GluFib peptide is investigated together with dodecylphosphocholine (DPC) micelles which were used for mimicking the environment of peptide in blood vessels. The spatial structure was obtained by applying 1D and 2D 1H-1H NMR spectroscopy (TOCSY, NOESY). It was shown that the fibrinopeptide B does not have a secondary structure but we can distinguish the fragment Gly 9 – Arg 14 with a good convergence (the backbone RMSD for the Gly9 – Arg14 is 0.18 ± 0.08 Å).

Place, publisher, year, edition, pages
2015. Vol. 1102, p. 91-94
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
Identifiers
URN: urn:nbn:se:ltu:diva-10069DOI: 10.1016/j.molstruc.2015.08.059ISI: 000364268300013Scopus ID: 2-s2.0-84940740609Local ID: 8d191bc8-839b-4596-889b-6396f7919377OAI: oai:DiVA.org:ltu-10069DiVA, id: diva2:983009
Note
Validerad; 2015; Nivå 2; 20150831 (andbra)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2018-07-10Bibliographically approved

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