Investigation of two blood proteins binding to Cantharidin and Norcantharidin by multispectroscopic and chemometrics methods
作者： Rong Liu , Zhengjun Cheng , Tian Li , Xiaohui Jiang
DOI: 10.1016/J.JLUMIN.2014.08.029
关键词: Blood proteins 、 Analytical chemistry 、 Quenching (fluorescence) 、 Bovine serum albumin 、 Chemometrics 、 CTD 、 Fluorescence 、 Chemistry 、 Norcantharidin 、 Absorption (pharmacology)
摘要: Abstract The interactions of Cantharidin/Norcantharidin (CTD/NCTD) with two blood proteins, i.e., bovine serum albumin (BSA) and hemoglobin (BHb), have been investigated by the fluorescence, UV–vis absorption, FT-IR spectra under imitated physiological condition. binding characteristics between CTD/NCTD BSA/BHb were determined fluorescence emission resonance light scattering (RLS) spectra. quenching mechanism proteins is a static quenching. Moreover, experimental data further analyzed based on multivariate curve resolution-alternating least squares (MCR-ALS) technique to obtain concentration profiles pure for three species (BSA/BHb, CTD/NCTD–BSA/BHb complexes) which existed in interaction procedure. number sites n constants K b calculated at various temperatures. thermodynamic parameters (such as, Δ G , H S ) BSA–CTD/NCTD BHb–CTD/NCTD systems Van’t Hoff equation also discussed. distance r evaluated according Forster no-radiation energy transfer theory. results Fourier transform infrared (FT-IR), synchronous three-dimensional showed that conformations altered addition CTD/NCTD. In addition, effects common ions
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