Synthesis, thermodynamic properties and BSA interaction of a new Valen Shiff base derived from o-vanillin and trimethoprim
| Autor: | Du-Gui He, Xia Li, Chuan-Hua Li, Jian-Hong Jiang, Li-Juan Ye, Sheng-Xiong Xiao, Fei-Hong Yao, Hui-Wen Gu, Qiang-Guo Li, Xu Li |
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| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
Isothermal microcalorimetry Chromatography Quenching (fluorescence) Base (chemistry) biology O-vanillin Condensed Matter Physics Acceptor Standard enthalpy of formation chemistry biology.protein Physical chemistry Physical and Theoretical Chemistry Bovine serum albumin Spectroscopy Instrumentation |
| Zdroj: | Thermochimica Acta. 575:291-299 |
| ISSN: | 0040-6031 |
| DOI: | 10.1016/j.tca.2013.11.015 |
| Popis: | a b s t r a c t A new Valen Shiff base (C22H24N4O5) was synthesized using equivalent moles of o-vanillin and trimetho- prim. At 298.15 K, the standard molar enthalpy of formation of the new compound was estimated to be � f H � m (C22H24N4O5(s), 298.15 K) = −(696.92 ± 1.67) kJ mol −1 by microcalorimetry. In particular, the inter- action between the Shiff base and bovine serum albumin (BSA) has been investigated. It was proved that the fluorescence quenching of BSA by Shiff base is a result of the formation of a Shiff base-BSA complex. Quenching constants were determined using the Sterns-Volmer equation to provide a measurement of the binding site between Shiff base and BSA. The thermodynamic parametersG, � H, andS of the sys- tem at different temperatures were calculated. What is more, the distance r between donor (Trp. 213) and acceptor (Shiff base) was obtained. Finally, synchronous fluorescence spectroscopy data has suggested the association between Shiff base and BSA changed the molecular conformation of BSA. © 2013 Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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