o-Alkylselenenylated Benzoic Acid Accesses Several Sites in Serum Albumin According to Fluorescence Studies, Raman Spectroscopy and Theoretical Simulations

Author(s): Federico Martinez-Ramos, Yadira Fonseca-Sabater, Marvin A. Soriano-Ursua, Eduardo Torres, Martha C. Rosales-Hernandez, Jose G. Trujillo-Ferrara, Luis E. Tolentino-Lopez, Ilizaliturri-Flores Ian, Jose Correa-Basurto.

Journal Name: Protein & Peptide Letters

Volume 20 , Issue 6 , 2013

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Abstract:

In the circulatory system, serum albumin (SA) is an important transporter of the majority of molecules with biological activity. We focused the current study on the anti-inflammatory compound, o-alkylselenenylated benzoic acid (ALKSEBEA), to determine its ability to access SA. Herein, we employed experimental procedures (fluorescence studies, Raman spectroscopy) and docking study on SA obtained from the Protein Data Bank and key conformers obtained from molecular dynamics simulations. The results show that ALKSEBEA accesses SA using a cooperative behavior according to fluorescence studies. In addition, the Raman results indicate that the ligand binding affects the backbone constituents. These results were confirmed by docking simulations tested on several SA conformers, which showed that ALKSEBEA bound on several sites on SA via π-π or π-cation interactions and that the ligand reaches other binding sites, where aromatic and basic residues as well as the backbone residues are involved.

Keywords: Serum albumin, selenium, fluorescence and Raman spectroscopy, molecular dynamics and docking simulations.

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Article Details

VOLUME: 20
ISSUE: 6
Year: 2013
Page: [705 - 714]
Pages: 10
DOI: 10.2174/0929866511320060009
Price: $65

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