作者: Yan-Qing Wang , Hong-Mei Zhang , Qiu-Hua Zhou
DOI: 10.1016/J.EJMECH.2008.10.010
关键词: Fluorescence 、 Chemistry 、 Fluorescence spectrometry 、 Chemical structure 、 Stability constants of complexes 、 Fluorescence spectroscopy 、 Hydrogen bond 、 Stereochemistry 、 Hemoglobin 、 Intermolecular force
摘要: Caffeine (CF) is a member of the methylxanthine family with numerous biological activities, which may contribute to prevention human disease but also be potentially harmful. In present study, interaction CF bovine hemoglobin (BHb) under physiological condition was studied by fluorescence and UV/vis spectroscopy. Fluorescence data revealed that quenching BHb result formed complex CF-BHb. The binding constants thermodynamic parameters at three different temperatures, position, force were determined. hydrophobic hydrogen bonds interactions predominant intermolecular forces stabilize complex. conformation discussed synchronous techniques. spectra indicated structures Tyr Try residues environments altered functions affected 0. This study provides important insight into mechanism erythrocyte sickling, useful guideline for further toxicology investigation.