Journal
JOURNAL OF LUMINESCENCE
Volume 130, Issue 3, Pages 360-364Publisher
ELSEVIER
DOI: 10.1016/j.jlumin.2009.09.020
Keywords
Prulifloxacin; Trypsin; Luminescence quenching; Stern-Volmer equation; The Forster resonance energy transfer theory
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Prulifloxacin is a kind of new oral taking antibiotic of fluoroquinolone. Conjugation reaction of prulifloxacin with trypsin in Britton-Robinson buffer solution of pH 7.96 was analyzed by UV-vis spectrophotometry and fluorescence spectrometry. The intrinsic fluorescence of trypsin was strongly quenched by prulifloxacin. This effect was rationalized in terms of a static quenching procedure. The binding parameters have been evaluated by fluorescence quenching methods. Negative values Delta G(0) for the formation of prulifloxacin-trypsin complex implied that both hydrogen bonds and hydrophobic interactions might play a significant role in prulifloxacin binding to trypsin. The binding distance deduced from the efficiency of energy transfer was 0.84 nm for prulifloxacin-trypsin. Furthermore, association constants and binding mechanism were successfully derived from the fluorescence spectra. UV-vis detections supported a change in the secondary structure of proteins caused by the interaction of prulifloxacin with trypsin. (C) 2009 Elsevier B.V. All rights reserved.
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