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Investigation on the Binding Interactions between Drugs and Bovine Serum Albumin with Affinity Chromatography and Fluorescence Spectroscopy

Author: ZengXiaoLei
Tutor: WeiYinMao
School: Northwestern University
Course: Analytical Chemistry
Keywords: Affinity Chromatography Fluorescence spectroscopy Bovine serum albumin (BSA) Berberine hydrochloride Chlorpromazine hydrochloride Propranolol hydrochloride
CLC: R96
Type: Master's thesis
Year: 2007
Downloads: 259
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Abstract

Albumin is the most abundant blood protein transport, the study drug and other small molecule ligands Albumin mechanism and the role of the process is of great significance in toxicology, pharmacokinetics. In this thesis, comprehensive utilization of cutting-edge analysis and fluorescence spectra of bovine serum albumin (BSA) and berberine hydrochloride (BC), chlorpromazine hydrochloride, propranolol hydrochloride, the interaction of the three drugs. The thesis consists of two parts: the forefront chromatography determined by a combination of three drugs with immobilized BSA role and effects of temperature, the pH of the mobile phase and the the additives affect it, the following conclusions: (1) BSA and chlorpromazine hydrochloride, propranolol hydrochloride, and BC at 30 ℃, the binding constant of 2.67 × 10 ~ 4,4.21 × 10 ~ 4 and 4.79 × 10 4L/mol binding rate greater than 80%, indicating that there is a strong interaction between these three drugs with BSA, they are able to BSA storage and transfer. (2) As the temperature increases, the three drugs are retained in the column of BSA reduced. BC and propranolol hydrochloride in the BSA column retention decreases the number of binding sites and the combined result of lower strength. Chlorpromazine hydrochloride reserved reduced mainly the result is a the BSA column of the total number of active sites decreases. (3) BC, propranolol hydrochloride and the BSA role in the process of △ G <0, ΔS> 0, △ H <0 Description BSA binding the main driving force for the electrostatic force. The process of chlorpromazine hydrochloride with BSA △ G <0, ΔS> 0, △ H> 0, hydrophobic interaction is the main driving force of their combined. (4) The pH of the solution increases, chlorpromazine hydrochloride and propranolol hydrochloride and BSA binding constant increases. The mobile phase isopropanol concentration increases, the binding constants of the two drugs and BSA are reduced, indicating that the hydrophobic force have a certain effect on the combination of drugs and BSA. The degree of reduction of chlorpromazine hydrochloride and BSA binding the main driving force is hydrophobic force. Second, the fluorescence method of the solution, chlorpromazine hydrochloride and BC and BSA interaction, and frontal chromatography results obtained were compared to the following conclusions: 1 chlorpromazine hydrochloride and BC and BSA the quenching static quenching and non-radiative energy transfer. 40 ° C when the two drugs and BSA binding constants were 1.45 × 10 ~ 4 and 6.56 × 10 4L/mol. 2 BC, hydrochloric acid, chlorpromazine and BSA was 1.89 and 1.27nm, indicating that they could be cutting into the hydrophobic cavity of BSA interact. The thermodynamic parameters, the main driving force of chlorpromazine hydrochloride and BSA binding force is hydrophobic, the main driving force for BC and BSA binding is static electricity. BSA and chlorpromazine hydrochloride three cutting-edge analysis and by fluorescence measured thermodynamic parameters and the BC binding constants and binding process in comparison to illustrate the behavior of a combination of two drugs with immobilized BSA in solution with BSA combination of similar behavior.

Investigation on the Binding Interactions between Drugs and Bovine Serum Albumin with Affinity Chromatography and Fluorescence Spectroscopy

Abstract

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