Journal
JOURNAL OF LUMINESCENCE
Volume 146, Issue -, Pages 114-122Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jlumin.2013.09.054
Keywords
Serum albumins; Citalopram; Spectroscopic methods; Binding affinity; Conformational change
Categories
Funding
- National Basic Research Program of China [2010CB933501]
- National Natural Science Foundation of China [20875055]
- Natural Science Foundation of Fujian Province, China [2013J01388]
- State Key Lab of Structural Chemistry, Fujian Institute of Research on the Structure of Matter
- Opening Research Foundation of Key Laboratory of Biomedical Material in Tianjin city
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The binding interactions of citalopram (CIT), an efficient antidepressant, with human serum albumin (HSA) and bovine serum albumin (BSA) were investigated by a series of spectroscopic methods including fluorescence, UV vis absorption, circular dichroism (CD) and H-1 nuclear magnetic resonance (H-1 NMR). The fluorescence quenching and UV vis absorption studies reveal that CIT could form complexes with both HSA and BSA. The CIT-BSA complex exhibits higher binding affinity than CIT HSA complex. The thermodynamic study further suggests that the interactions between CIT and SAs are mainly driven by hydrophobic forces and hydrogen bonds. The 1H NMR analysis indicates that the participation of different functional groups of CIT is unequal in the complexation of CIT HSA and CIT BSA. Site marker competitive experiments show that the interactions between CIT and SAs primarily locate at sub-domain II A (site I). The effects of CIT on the conformation of SAs are further analyzed via synchronous fluorescence, three-dimensional fluorescence and CD spectra techniques. The results prove that the presence of CIT decreases the alpha-helical content of both SAs and induces the slight unfolding of the polypeptides of protein. Additionally, the conformational change of BSA induced by CIT is larger than that of HSA. (C) 2013 Elsevier B.V. All rights reserved.
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