Publications by authors named "Xin-Min Jiang"

Article Synopsis
  • The study investigates how sorbitol interacts with bovine serum albumin (BSA) using fluorescence and UV absorption techniques, which is significant for understanding drug interactions with biological molecules.
  • The findings indicate that sorbitol significantly reduces the fluorescence of BSA through a static quenching mechanism, which can vary with temperature and drug concentration, and this is supported by changes in absorption spectra.
  • The research also calculates binding constants and thermodynamic parameters, revealing that the primary interaction between sorbitol and BSA is driven by electrostatic forces and that sorbitol may affect BSA's structure, particularly around the tyrosine residues.
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In the present paper, a fluorescence method was used to study at different pH the fluorescence quenching of bovine serum albumin (BSA) by its interaction with balofloxacin (BLFX). The interaction association constants of BSA and BLFX were determined from a double reciprocal line Weaver-Burk plot. According to the Forster dipole-dipole energy transfer, the distance to be measured between the BLFX and tryptophane is 5.

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