A circular dichroism study of (+) gossypol binding to proteins

Sampath, DS and Whaley, Kevin J and Balaram, P (1984) A circular dichroism study of (+) gossypol binding to proteins. In: Biochemical and Biophysical Research Communications, 121 (3). 953 -959.

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Abstract

The circular dichroism bands of (+) gossypol in the spectral region 300–400 nm have been shown to be sensitive to interactions with proteins. Using CD spectroscopy, gossypol has been shown to interact with lactate dehydrogenase, malate dehydrogenase, alkaline phosphatase, lysozyme, protamine and poly-L-lysine. Binding to proteins generally results in a pronounced red shift of the long wavelength CD band (not, vert, similar 380–430 nm) accompanied by a reduction in ellipticity. The changes in spectral parameters of the 1Lb binaphthyl transtion may reflect a distortion from a nearly perpendicular gossypol conformation, on binding to proteins.

Item Type:	Journal Article
Publication:	Biochemical and Biophysical Research Communications
Publisher:	Elsevier Science
Additional Information:	Copyright for this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	03 Sep 2009 17:40
Last Modified:	19 Sep 2010 05:43
URI:	http://eprints.iisc.ac.in/id/eprint/22873

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