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o-Alkylselenenylated benzoic acid accesses several sites in serum albumin according to fluorescence studies, Raman spectroscopy and theoretical simulations.


Protein Pept Lett. 2012 Sep 4;


Authors: Martinez-Ramos F, Fonseca-Sabater Y, Soriano-Ursúa MA, Torres E, Rosales-Hernández MC, Trujillo-Ferrara JG, Tolentino-Lopez LE, Ian IF, Correa-Basurto J


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 properties. These results were confirmed by docking simulations tested on several SA conformers, which showed that ALKSEBEA bound 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.

PMID: 22973844 [PubMed - as supplied by publisher]