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BioMed Research International
Volume 2014 (2014), Article ID 872701, 6 pages
Research Article

Morphological Analysis and Interaction of Chlorophyll and BSA

Grupo de Materiais Nanoestruturados, Universidade Federal de Mato Grosso, 78600-000 Barra do Garças, MT, Brazil

Received 27 February 2014; Revised 21 April 2014; Accepted 21 April 2014; Published 18 May 2014

Academic Editor: Rumiana Koynova

Copyright © 2014 Filipe D. S. Gorza et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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 (~104 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.