MICHALCOVÁ, Lenka and Zdeněk GLATZ. Comparison of various capillary electrophoretic approaches for the study of drug–protein interaction with emphasis on minimal consumption of protein sample and possibility of automation. JOURNAL OF SEPARATION SCIENCE. 2015, vol. 38, No 2, p. 325-331. ISSN 1615-9306. doi:10.1002/jssc.201400914.
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Basic information
Original name Comparison of various capillary electrophoretic approaches for the study of drug–protein interaction with emphasis on minimal consumption of protein sample and possibility of automation
Authors MICHALCOVÁ, Lenka (203 Czech Republic, belonging to the institution) and Zdeněk GLATZ (203 Czech Republic, guarantor, belonging to the institution).
Edition JOURNAL OF SEPARATION SCIENCE, 2015, 1615-9306.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Germany
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 2.741
RIV identification code RIV/00216224:14310/15:00080618
Organization unit Faculty of Science
Doi http://dx.doi.org/10.1002/jssc.201400914
UT WoS 000348516600020
Keywords in English Affinity capillary electrophoresis; Binding constants; Frontal analysis; Hummel Dreyer method; Thermodynamic parameters;
Tags AKR, rivok
Tags International impact, Reviewed
Changed by Changed by: Ing. Andrea Mikešková, učo 137293. Changed: 29/3/2016 15:49.
Abstract
The binding ability of a drug to plasma proteins influences the pharmacokinetics of a drug. As a result, it is a very important issue in new drug development. In this study, affinity capillary electrophoresis, capillary electrophoresis with frontal analysis, and Hummel Dreyer methods with internal and external calibration were used to study the affinity between bovine serum albumin and salicylic acid. The binding constant was measured by all these approaches including the equilibrium dialysis, which is considered to be a reference method. The comparison of results and other considerations showed the best electrophoretic approach to be capillary electrophoresis-frontal analysis, which is characterized by the high sample throughput with the possibility of automation, very small quantities of biomacromolecules, simplicity, and a short analysis time. The mechanism of complex formation was then examined by capillary electrophoresis with frontal analysis. The binding parameters were determined and the corresponding thermodynamic parameters such as Gibbs free energy G0, enthalpy H0, and entropy S0 changes at various temperatures were calculated. The results showed that the binding of bovine serum albumin and salicylic acid was spontaneous, and that hydrogen bonding and van der Waals forces played a major role in the formation of the complex.
Links
GBP206/12/G014, research and development projectName: Centrum pokročilých bioanalytických technologií
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