albumin - publications

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1. J Photochem Photobiol B. 2012 Apr 19. [Epub ahead of print]

Molecular spectroscopic studies on the interaction of morin with bovine serum
albumin.

Hu YJ, Yue HL, Li XL, Zhang SS, Tang E, Zhang LP.

Hubei Key Laboratory of Pollutant Analysis & Reuse Technology, Department of
Chemistry, Hubei Normal University, Huangshi 435002, PR China.

The interaction between morin and bovine serum albumin (BSA) was studied using
molecular spectroscopic approach at different temperatures under imitated
physiological conditions. Quenching of intrinsic tryptophanyl fluorescence of BSA
with increasing morin concentration is the actuating tool in the analysis. The
obtained quenching mechanisms, binding constants, binding sites and corresponding
thermodynamic parameters at different temperatures indicate that the hydrophobic
interaction play a major role in the morin-BSA association. Binding affinity
between morin and BSA was determined using Scatchard equation and the modified
Stern-Volmer equation, and the corresponding Structure-affinity relationships of
flavonoids were discussed. Site marker competitive displacement experiments
demonstrated that morin binds with high affinity to site II (subdomain IIIA) of
BSA. Furthermore, the circular dichroism spectral results indicated that the
conformation of BSA changed in the presence of morin. In addition, the effect of
some common metal ions on the binding constant between morin and BSA was
examined.

Copyright © 2012 Elsevier B.V. All rights reserved.

PMID: 22564497 [PubMed - as supplied by publisher]