Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 78, Issue 4, Pages 1278-1286Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2010.12.077
Keywords
Interaction; Bovine serum albumin (BSA); o-Vanillin Schiff Bases; Fluorescence spectroscopy
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Funding
- National Natural Science Foundation of China
- Liaoning Province Natural Science Foundation of Education Department
- Liaoning Province Natural Science Foundation of Science and Technology Department
- Liaoning University 211 Engineering Construction Foundation
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In this work, three o-Vanillin Schiff Bases (o-VSB: o-Vanillin-D-Phenylalanine (o-VDP), o-Vanillin-L-Tyrosine (o-VLT) and o-Vanillin-L-Levodopa (o-VLL)) with alanine constituent were synthesized by direct reflux method in ethanol solution, and then were used to study the interaction to bovine serum albumin (BSA) molecules by fluorescence spectroscopy. Based on the fluorescence quenching calculation, the bimolecular quenching constant (K-q), apparent quenching constant (K-sv), effective binding constant (K-A) and corresponding dissociation constant (K-D) as well as binding site number (n) were obtained. In addition, the binding distance (r) was also calculated according to Foster's non-radioactive energy transfer theory. The results show that these three o-VSB can efficiently bind to BSA molecules, but the binding array order is o-VDP-BSA > o-VLT-BSA > o-VLL-BSA. Synchronous fluorescence spectroscopy indicates that the o-VDP is more accessibility to tryptophan (Trp) residues of BSA molecules than to tyrosine (Tyr) residues. Nevertheless, the o-VLT and o-VLL are more accessibility to Tyr residues than to Trp residues. (C) 2010 Elsevier B.V. All rights reserved.
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