albumin - publications

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1. J Pharm Biomed Anal. 2012 Apr 17. [Epub ahead of print]

Combined fluorescence spectroscopy and molecular modeling studies on the
interaction between harmalol and human serum albumin.

Hemmateenejad B, Shamsipur M, Samari F, Khayamian T, Ebrahimi M, Rezaei Z.

Department of Chemistry, Shiraz University, Shiraz, Iran.

The interaction between harmalol and human serum albumin (HSA) has been studied
by fluorescence spectroscopy and molecular modeling methods. The intrinsic
fluorescence of HSA was quenched by harmalol, which was rationalized in terms of
the static quenching mechanism. The binding parameters, quenching constants and
conformation changes were determined by fluorescence quenching method. The
thermodynamic parameters, calculated from the temperature dependence of binding
constants (i.e., ΔH°=-62.7kJmol(-1) and ΔS°=-119.3Jmol(-1)K(-1)), indicated the
major role of van der Waals force and hydrogen bonding in binding process. Site
marker competitive experiments revealed that harmalol binds to both the IIA and
IIIA sub-domains of HSA with a slight preference toward sub-domain IIA. Finally,
the binding of harmalol to HSA was modeled by molecular docking and molecular
dynamic simulation methods. Excellent agreement was found between the
experimental and theoretical results with respect to the mechanism of binding and
binding constants. Molecular dynamic simulation revealed that HSA does not have a
significant conformational change when it binds with harmalol.

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

PMID: 22560122 [PubMed - as supplied by publisher]