Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5403439 | Journal of Luminescence | 2008 | 6 Pages |
Abstract
The binding of pazufloxacin mesilate (PZFX) to human serum albumin (HSA) or lysozyme (Lys) was investigated using spectrophotometric techniques. The intrinsic fluorescence of both HSA and Lys was strongly quenched by PZFX. This effect was rationalized in terms of a static quenching procedure. Negative values of ÎH0 and ÎS0 for the formation of PZFX-HSA or PZFX-Lys complex implied that both hydrogen bonds and hydrophobic interactions might play a significant role in PZFX binding to HSA or Lys. The binding distances deduced from the efficiency of energy transfer were 4.04 and 3.21Â nm for PZFX-HSA and PZFX-Lys systems, respectively. Furthermore, association constants and binding mechanism were successfully derived from the synchronous fluorescence spectra. Circular dichroism (CD) spectra and UV/vis detections supported a change in the secondary structure of proteins caused by the interaction of PZFX with HSA or Lys.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Jing Jin, Xia Zhang,