Synthesis Of Novel Oxodiazoles And Study On Interaction Of Serum Albumin With Them By Spectrometry

Serum albumin(SA) is an abundant protein closely related to drug storage andtransport in animals, therefore, it has great positive and practical significance toresearch the interaction between serum albumin and drugs. Meanwhile, theconclusions have certain guiding meaning to the subjects of pharmacokinetics,pharmacological properties and biochemistry.1,3,4-Oxadiazolines derivatives show a broad range of biological activityincluding insecticidal, fungicidal, anti-HIV and anti-convulsive, therefore, the studyof serum albumin and oxazoline drugs plays an important role in understanding theabsorption, distribution, combination of metabolic, pharmacological activity andtoxicity of oxazoline drugs in the human body. We outlined the theoreticalsignificance of the interaction between BSA and small molecule substances andsummarized the latest national and international work in the beginning of this article.And then, learnt from the known results and related literature, we have designed andsynthesized three novel oxodiazoles. Meanwhile, the interaction of three smallmolecule substances with BSA and HSA was investigated using UV-Visibleabsorption spectroscopy combined with fluorescence spectroscopy. The followingare the main results:1. Synthesis of three novel oxodiazoles and characterised by1HNMR,13CNMR and IR.2. The interaction of NPDO with human serum albumin(HSA) and bovineserum albumin (BSA) under physiological pH7.4conditions has been investigatedby fluorescence spectroscopy. The experimental results indicated that thefluorescence quenching mechanism was static quenching procedure. The bindingsites number, the binding constant K and the thermodynamic parameters at differenttemperatures were measured, which indicated that the action force was mainlyhydrogen bonds and van der Waals interactions. Based on the F ster non-radioactiveenergy transfer theory, the distance r between donor (BSA and HSA) and acceptor(NPDO) has been calculated. In addition, UV-Visible absorption the synchronous and3-D fluorescence spectra were explored to studied the effect of NPDO on theconformation of BSA and HSA, compare size of the binding capercity of the PNDOwith BSA and HSA.,.3. The interaction of MPNDO with human serum albumin(HSA) and bovineserum albumin (BSA) under physiological pH7.4conditions has been investigatedby fluorescence spectroscopy. The experimental results indicated that thefluorescence quenching mechanism was static quenching procedure. The bindingsites number, the binding constant K and the thermodynamic parameters at differenttemperatures were measured, which indicated that the action force was mainlyhydrogen bonds and van der Waals interactions. Based on the F ster non-radioactiveenergy transfer theory, the distance r between donor (BSA and HSA) and acceptor(MNPDO) has been calculated. In addition, UV-Visible absorption the synchronousand3-D fluorescence spectra were explored to studied the effect of MPNDO on theconformation of BSA and HSA, compare size of the binding capercity of theMPNDO with BSA and HSA..4. The interaction of MOPNDO with human serum albumin(HSA) and bovineserum albumin (BSA) under physiological pH7.4conditions has been investigatedby fluorescence spectroscopy. The experimental results indicated that thefluorescence quenching mechanism was static quenching procedure. The bindingsites number, the binding constant K and the thermodynamic parameters at differenttemperatures were measured, which indicated that the action force was mainlyhydrogen bonds and van der Waals interactions. Based on the F ster non-radioactiveenergy transfer theory, the distance r between donor (BSA and HSA) and acceptor(MOPNDO) has been calculated. In addition, UV-Visible absorption thesynchronous and3-D fluorescence spectra were explored to studied the effect ofMOPNDO on the conformation of BSA and HSA, compare size of the bindingcapercity of the MOPNDO with BSA and HSA.