Journal
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
Volume 139, Issue -, Pages 109-115Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jpba.2017.02.050
Keywords
Colon cancer; Fluorescence quenching; Irinotecan; Beta-Lactoglobulin; Non-radiative energy transfer; Partial compactness
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Funding
- Research Councils of Razi University
- Kermanshah University of Medical Sciences [94048]
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The binding of irinotecan, a potent anti cancer drug, to bovine beta-lactoglobulin (beta-LG) was investigated by various spectroscopic techniques including fluorimetry, circular dichroism (CD), UV-vis, and Fourier transform infrared (FT-IR), in 10 mM phosphate buffer, pH 7.75, in combination with a molecular docking study. Analysis of the fluorescence quenching data showed that combined static and dynamic quenching occurs, with the predominant contribution of the static mode. Molecular docking results were in full agreement with the results obtained from thermodynamic analysis of the fluorescence data indicating the existence of one binding site for irinotecan in beta-LG structure and revealed the hydrophobic nature of the interaction between irinotecan and the protein. The binding distance between beta-LG and irinotecan, r, was estimated to be 5.74 nm based on the Forster's theory of non-radiative energy transfer. The obtained results of near-UV CD and FT-IR experiments suggested the occurrence of partial compactness of the protein structure upon irinotecan binding. Based on the experimental data and the possible binding mode revealed by molecular docking study, we concluded that irinotecan binds to the hydrophobic calyx of beta-LG with induction of some alterations in the secondary and tertiary structure of the protein. (C) 2017 Elsevier B.V. All rights reserved.
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