Morphological analysis and interaction of chlorophyll and BSA.

Abstract:

:Interactions between proteins and drugs, which can lead to formation of stable drug-protein complexes, have important implications on several processes related to human health. These interactions can affect, for instance, free concentration, biological activity, and metabolism of the drugs in the blood stream. Here, we report on the UV-Visible spectroscopic investigation on the interaction of bovine serum albumin (BSA) with chlorophyll (Chl) in aqueous solution under physiological conditions. Binding constants at different temperatures--obtained by using the Benesi-Hildebrand equation--were found to be of the same order of magnitude (~10(4)M(-1)) indicating low affinity of Chl with BSA. We have found a hyperchromism, which suggested an interaction between BSA and Chl occurring through conformational changes of BSA caused by exposition of tryptophan to solvent. Films from BSA and Chl obtained at different Chl concentrations showed fractal structures, which were characterized by fractal dimension calculated from microscopic image analysis.

journal_name

Biomed Res Int

authors

Gorza FD,Pedro GC,Trescher TF,da Silva RJ,Silva JR,de Souza NC

doi

10.1155/2014/872701

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

872701

eissn

2314-6133

issn

2314-6141

journal_volume

2014

pub_type

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