albumin - publications

Predict more albumin - ligand interactions now!


1. Chemphyschem. 2012 Apr 24. doi: 10.1002/cphc.201200044. [Epub ahead of print]

Comparative Study of Flavins Binding with Human Serum Albumin: A Fluorometric,
Thermodynamic, and Molecular Dynamics Approach.

Sengupta A, Sasikala WD, Mukherjee A, Hazra P.

Department of Chemistry, Indian Institute of Science Education and Research
(IISER), Pune, Pune 411021, Maharashtra (India).

Flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) are derivatives
of riboflavin (RF), a water-soluble vitamin, more commonly known as vitamin B(2)
. Flavins have attracted special attention in the last few years because of the
recent discovery of a large number of flavoproteins. In this work, these flavins
are used as extrinsic fluorescence markers for probing the microheterogeneous
environment of a well-known transport protein, human serum albumin (HSA).
Steady-state and time-resolved fluorescence experiments confirm that both FMN and
FAD bind to the Sudlow's site-1 (SS1) binding pocket of HSA, where Trp214
resides. In the case of RF, a fraction of RF molecules binds at the SS1, whereas
the major fraction of RF molecules remains unbound or surface bound to the
protein. Moreover, flavin(s)-HSA interactions are monitored with the help of
isothermal titration calorimetry, which provides free energy, enthalpy, and
entropy changes of binding along with the binding constants. The molecular
picture of binding interaction between flavins and HSA is well explored by
docking and molecular dynamics studies.

Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

PMID: 22532419 [PubMed - as supplied by publisher]