MICHALCOVÁ, Lenka a 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, roč. 38, č. 2, s. 325-331. ISSN 1615-9306. doi:10.1002/jssc.201400914.
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Základní údaje
Originální název 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
Autoři MICHALCOVÁ, Lenka (203 Česká republika, domácí) a Zdeněk GLATZ (203 Česká republika, garant, domácí).
Vydání JOURNAL OF SEPARATION SCIENCE, 2015, 1615-9306.
Další údaje
Originální jazyk angličtina
Typ výsledku Článek v odborném periodiku
Obor 10600 1.6 Biological sciences
Stát vydavatele Německo
Utajení není předmětem státního či obchodního tajemství
Impakt faktor Impact factor: 2.741
Kód RIV RIV/00216224:14310/15:00080618
Organizační jednotka Přírodovědecká fakulta
Doi http://dx.doi.org/10.1002/jssc.201400914
UT WoS 000348516600020
Klíčová slova anglicky Affinity capillary electrophoresis; Binding constants; Frontal analysis; Hummel Dreyer method; Thermodynamic parameters;
Štítky AKR, rivok
Příznaky Mezinárodní význam, Recenzováno
Změnil Změnila: Ing. Andrea Mikešková, učo 137293. Změněno: 29. 3. 2016 15:49.
Anotace
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.
Návaznosti
GBP206/12/G014, projekt VaVNázev: Centrum pokročilých bioanalytických technologií
VytisknoutZobrazeno: 7. 12. 2022 13:27