ArticleMolecular biology reports2013
Biophysical studies on the interactions of jatrorrhizine with bovine serum albumin by spectroscopic and molecular modeling methods.
Article in Molecular biology reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 12 citations in OpenAlex.
- Natural isoquinoline alkaloids: binding aspects to functional proteins, serum albumins, hemoglobin, and lysozyme.Biophysical reviews · 2015Review
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Authors and funding
7 authors at 2 institutions in 1 country.
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Abstract
The interaction between jatrorrhizine (JAT) and bovine serum albumin (BSA) has been studied. The studies were carried out in a buffer medium at pH 7.4 using fluorescence spectroscopy, UV-vis spectroscopy, and molecular modeling methods. The results of fluorescence quenching and UV-vis absorption spectra experiments indicated the formation of the complex of BSA-JAT. Binding parameters were determined using the Stern-Volmer equation and Scatchard equation. The results of thermodynamic parameters ΔG, ΔH and ΔS at different temperatures indicate that the electrostatic interactions and hydrogen bonds play a major role for JAT-BSA association. Site marker competitive displacement experiments and molecular modeling calculation demonstrating that JAT is mainly located within the hydrophobic pocket of the subdomain IIIA of BSA. Furthermore, The distance between donor (BSA) and acceptor (JAT) was estimated according to fluorescence resonance energy transfer.
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