TY - JOUR
T1 - O-alkylselenenylated benzoic acid accesses several sites in serum albumin according to fluorescence studies, Raman spectroscopy and theoretical simulations
AU - Martinez-Ramos, Federico
AU - Fonseca-Sabater, Yadira
AU - Soriano-Ursúa, Marvin A.
AU - Torres, Eduardo
AU - Rosales-Hernández, Martha C.
AU - Trujillo-Ferrara, José G.
AU - Tolentino-Lopez, Luis E.
AU - Ian, Ilizaliturri Flores
AU - Correa-Basurto, José
PY - 2013/6
Y1 - 2013/6
N2 - 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 β-β or β-cation interactions and that the ligand reaches other binding sites, where aromatic and basic residues as well as the backbone residues are involved.
AB - 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 β-β or β-cation interactions and that the ligand reaches other binding sites, where aromatic and basic residues as well as the backbone residues are involved.
KW - Fluorescence and Raman spectroscopy
KW - Molecular dynamics and docking simulations
KW - Selenium
KW - Serum albumin
UR - http://www.scopus.com/inward/record.url?scp=84877957753&partnerID=8YFLogxK
U2 - 10.2174/0929866511320060009
DO - 10.2174/0929866511320060009
M3 - Artículo
SN - 0929-8665
VL - 20
SP - 705
EP - 714
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
IS - 6
ER -