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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Li, Junfen Dong, Chuan Li, Jinzeng Jiao, Yong |
| Description | Author Affiliation: Li J ( Institute of Chemistry and Chemical Engineering, Shanxi University, Taiyuan 030006, PR China.) |
| Abstract | In this work, the interaction of jatrorrhizine with human serum albumin (HSA) was studied by means of UV-vis and fluorescence spectra. The intrinsic fluorescence of HSA was quenched by jatrorrhizine, which was rationalized in terms of the static quenching mechanism. The results show that jatrorrhizine can obviously bind to HSA molecules. According to fluorescence quenching calculations, the bimolecular quenching constant (kq), apparent quenching constant (KSV) at different temperatures were obtained. The binding constants K are 4059 L mol(-1) and 1438 L mol(-1) at 299 K and 304 K respectively, and the number of binding sites n is almost 1. The thermodynamic parameters determined by the Van't Hoff analysis of the binding constants (ΔH -12.25 kJ mol(-1) and ΔS 28.17 J mol(-1) K(-1)) clearly indicate that the electrostatic force plays a major role in the process. The efficiency of energy transfer and the distance between the donor (HSA) and the acceptor (jatrorrhizine) were calculated as 22.2% and 3.19 nm according to Föster's non-radiative energy transfer theory. In addition, synchronous fluorescence spectroscopy reveals that jatrorrhizine can influence HSA's microstructure. That is, jatrorrhizine is more vicinal to tryptophane (Trp) residue than to tyrosine (Tyr) residue and the damage site is also mainly at Trp residue. Molecular modeling result shows that jatrorrhizine-HSA complex formed not only on the basis of electrostatic forces, but also on the basis of π-π staking and hydrogen bond. The research results will offer a reference for the studies on the biological effects and action mechanism of small molecule with protein. |
| ISSN | 13861425 |
| Volume Number | 118 |
| e-ISSN | 18733557 |
| Journal | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2014-01-24 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Berberine Analogs & Derivatives Models, Molecular Serum Albumin Chemistry Metabolism Binding Sites Energy Transfer Humans Kinetics Solutions Spectrometry, Fluorescence Temperature Journal Article Research Support, Non-u.s. Gov't Discipline Spectroscopy |
| Content Type | Text |
| Resource Type | Article |
| Subject | Spectroscopy Atomic and Molecular Physics, and Optics Analytical Chemistry Instrumentation |
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