1. Spectroscopic investigation of the interaction of water-soluble azocalix[4]arenes with bovine serum albumin.
- Author
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Fan, Ping, Wan, Lu, Shang, Yunshan, Wang, Jun, Liu, Yulong, Sun, Xiaoyu, and Chen, Chen
- Subjects
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CALIXARENE derivatives , *SERUM albumin , *WATER , *FLUORESCENCE spectroscopy , *AROMATIC compound synthesis , *NUCLEAR magnetic resonance spectroscopy , *FLUORESCENCE quenching - Abstract
In this work, three hydrosoluble azocalix[4]arene derivatives, 5-( o -methylphenylazo)-25,26,27-tris(carboxymethoxy)-28-hydroxycalix[4]arene ( o- MAC-Calix), 5-( m -methylphenylazo)-25,26,27-tris(carboxymethoxy)-28-hydroxycalix[4]arene ( m -MAC-Calix) and 5-( p -methylphenylazo)-25,26,27-tris(carboxymethoxy)-28-hydroxycalix[4]arene ( p -MAC-Calix) were synthesized. Their structures were characterized by infrared spectrum (IR), nuclear magnetic resonance spectrum ( 1 H NMR and 13 C NMR) and mass spectrum (MS). The interactions between these compounds and bovine serum albumin (BSA) were studied by fluorescence spectroscopy, UV–vis spectrophotometry and circular dichroic spectroscopy. According to experimental results, three azocalix[4]arene derivatives can efficiently bind to BSA molecules and the o -MAC-Calix displays more efficient interactions with BSA molecules than m -MAC-Calix and p -MAC-Calix. Molecular docking showed that the o -MAC-Calix was embedded in the hydrophobic cavity of helical structure of BSA molecular and the tryptophan (Trp) residue of BSA molecular had strong interaction with o -MAC-Calix. The fluorescence quenching of BSA caused by azocalix[4]arene derivatives is attributed to the static quenching process. In addition, the synchronous fluorescence spectroscopy indicates that these azocalix[4]arene derivatives are more accessible to Trp residues of BSA molecules than the tyrosine (Tyr) residues. The circular dichroic spectroscopy further verified the binding of azocalix[4]arene derivatives and BSA. [ABSTRACT FROM AUTHOR]
- Published
- 2015
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