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Self-diffusion in a hyaluronic acid–albumin–water system as studied by NMR
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0002-6810-1882
Kazan (Volga Region) Federal University, Kazan.
Kazan (Volga Region) Federal University, Kazan.
Kazan (Volga Region) Federal University, Kazan.
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2012 (English)In: Magnetic Resonance in Chemistry, ISSN 0749-1581, E-ISSN 1097-458X, Vol. 50, no 2, p. 114-119Article in journal (Refereed) Published
Abstract [en]

In the presence of even a small amount of hyaluronic acid, the self-diffusion coefficient of albumin decreases. Three hypotheses were proposed and analyzed. The most likely one is that BSA and HA molecules form complex. The state of the BSA molecules in the BSA-HA-D2O system corresponds to a ‘fast exchange’ condition from the NMR point of view: BSA molecules reside in the ‘free’ and ‘bound’ states for much shorter time than the diffusion time of the PFG NMR experiment. Hyaluronic acid (HA) is an anionic biopolymer that is present in many tissues and can be involved in cancerous neoformations. HA can form complexes with proteins (particularly, serum albumin) in the body. However, HA structures and processes involving HA have not been extensively studied by NMR because the molecule's rigid structure makes these studies problematic. In the current work, self-diffusion of HA and bovine serum albumin (BSA), and water in solutions was measured by 1H pulsed field gradient NMR (PFG NMR) with a focus on the HA-BSA-D2O systems at various concentrations of BSA and HA. It was shown that in the presence of even a small amount of HA, the self-diffusion coefficient (SDC) of BSA decreases. To explain this fact, three hypotheses were proposed and analyzed. The first one was based on the effect of slowing down of water mobility in the presence of HA. The second hypothesis suggested an effect of mechanical collisions of BSA with HA molecules. The third hypothesized that BSA and HA molecules form a complex where BSA molecules reduced in mobility. It was shown that the third mechanism is the most likely. The state of the BSA molecules in the BSA-HA-D2O system corresponds to a ‘fast exchange’ condition from the NMR point of view: BSA molecules reside in the ‘free’ and ‘bound’ (with HA) states for much shorter time than the diffusion time of the PFG NMR experiment, 7 ms. The fractions of ‘bound’ BSA molecules in the BSA-HA complex were estimated.

Place, publisher, year, edition, pages
2012. Vol. 50, no 2, p. 114-119
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
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URN: urn:nbn:se:ltu:diva-7857DOI: 10.1002/mrc.2853ISI: 000301235100004PubMedID: 22336898Scopus ID: 2-s2.0-84858340161Local ID: 64817589-3592-4522-a49c-fa4cd701dbb8OAI: oai:DiVA.org:ltu-7857DiVA, id: diva2:980747
Note
Validerad; 2012; 20120217 (andbra)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2018-07-10Bibliographically approved

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