albumin - publications

Predict more albumin - ligand interactions now!

1. Magn Reson Chem. 2012 Feb 15. doi: 10.1002/mrc.2853. [Epub ahead of print]

Self-diffusion in a hyaluronic acid-albumin-water system as studied by NMR.

Filippov A, Artamonova M, Rudakova M, Gimatdinov R, Skirda V.

Kazan (Volga Region) Federal University, Kazan, Russia; Luleå University of
Technology, Luleå, Sweden.

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 (1) H pulsed field gradient NMR (PFG NMR) with a focus on the
HA-BSA-D(2) O 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-D(2) O 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.
Copyright © 2012 John Wiley & Sons, Ltd.

Copyright © 2012 John Wiley & Sons, Ltd.

PMID: 22336898 [PubMed - as supplied by publisher]