Interaction of coumarin derivatives with human serum albumin: investigation by fluorescence spectroscopic technique and modeling studies

Shobini, J and Mishra, AK and Sandhya, K and Chandra, Nagasuma (2001) Interaction of coumarin derivatives with human serum albumin: investigation by fluorescence spectroscopic technique and modeling studies. In: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 57 (5). pp. 1133-1147.

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Abstract

Interactions of several 7-aminocoumarins with human serum albumin (HSA) were studied by using fluorescence spectroscopic technique and modeling studies. There is a large change in fluorescence spectral parameters like intensity, emission maxima and anisotropy for all aminocoumarins. There were two binding sites for cou-1, 311 and a single binding site for other coumarins. The binding constant(s) are large for all coumarins reflective of a strong binding. These spectral studies show that structural variants at the third, fourth and seventh position affects binding. The probable location of these coumarins in domain Ii has been predicted based on modeling. The effect of structural modification on the efficiency of binding was obtained for various other coumarins, using modeling.

Item Type:	Journal Article
Publication:	Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Keywords:	Human serum albumin;Coumarin;Modeling;Docking;Binding site
Department/Centre:	Division of Information Sciences (Doesn't exist now) > BioInformatics Centre
Date Deposited:	25 Aug 2009 12:49
Last Modified:	19 Sep 2010 04:55
URI:	http://eprints.iisc.ac.in/id/eprint/17050

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