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Spatial structure of heptapeptide Aβ 16-22 (beta-amyloid Aβ 1-40 active fragment) in solution and in complex with a biological membrane model
Kazan (Volga Region) Federal University, Kazan.
Kazan (Volga Region) Federal University, Kazan.
Kazan (Volga Region) Federal University, Kazan.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0002-6810-1882
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2012 (English)In: Magnetic Resonance in Chemistry, ISSN 0749-1581, E-ISSN 1097-458X, Vol. 50, no 12, p. 784-792Article in journal (Refereed) Published
Abstract [en]

The spatial structure of an active fragment of beta-amyloid Aβ 1-40 heptapeptide Aβ 16-22 (Lys-Leu-Val-Phe-Phe-Ala-Glu) in aqueous buffer solution and in complex with sodium dodecyl sulfate micelles as a model membrane system was investigated by 1H NMR spectroscopy and two-dimensional NMR (TOCSY, HSQC-HECADE (Heteronuclear Couplings from ASSCI-domain experiments with E.COSY-type crosspeaks), NOESY) spectroscopy. Complex formation was confirmed by the chemical shift changes of the heptapeptide's 1H NMR spectra, as well as by the signs and values of the NOE effects in different environments. We compared the spatial structure of the heptapeptide in borate buffer solution and in complex with a model of the cell surface membrane

Place, publisher, year, edition, pages
2012. Vol. 50, no 12, p. 784-792
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
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URN: urn:nbn:se:ltu:diva-7167DOI: 10.1002/mrc.3880ISI: 000311378700002Scopus ID: 2-s2.0-84869879158Local ID: 57de82dc-ee2b-4a40-86df-82c149a8b45cOAI: oai:DiVA.org:ltu-7167DiVA, id: diva2:980055
Note
Validerad; 2012; 20121010 (andbra)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2018-07-10Bibliographically approved

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Filippov, AndreiAntzutkin, Oleg

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