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Wyświetlanie 1-3 z 3
Tytuł:
Optical Spectroscopy Study of the Interaction Between Quercetin and Human Serum Albumin
Autorzy:
Wybranowski, T.
Kruszewski, S.
Powiązania:
https://bibliotekanauki.pl/articles/1197523.pdf
Data publikacji:
2014-04
Wydawca:
Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:
87.64.K-
87.64.kv
87.15.kp
Opis:
Optical methods are very useful for the study on behavior of molecules in albumin-containing solutions. The interaction between quercetin (QUE) and human serum albumin (HSA) under physiological conditions was investigated by the methods of UV-Vis absorption and fluorescence spectroscopy. Fluorescence data show that enhancing of quercetin fluorescence in the presence of HSA is the result of formation of the HSA-QUE complex. On the basis of fluorescence data, the binding affinity constant of quercetin to HSA is determined. In this paper we have attempted to perform a kinetic study of the oxidation of quercetin in presence of human serum albumin by absorption spectroscopy. It has been shown that quercetin easily oxidizes at pH 7.4. The addition of HSA to quercetin solution induces changes in the absorption spectrum. In the human serum albumin solution, the time of quercetin oxidation is longer than in the case of quercetin diluted in phosphate buffered saline. Human albumin also contributes to stabilization of quercetin. These results suggest that HSA prevents degradation of quercetin in blood.
Źródło:
Acta Physica Polonica A; 2014, 125, 4A; A-57-A-60
0587-4246
1898-794X
Pojawia się w:
Acta Physica Polonica A
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Fluorescence Spectroscopy in Camptothecins Studies
Autorzy:
Kruszewski, S.
Kruszewska, D.
Powiązania:
https://bibliotekanauki.pl/articles/1537476.pdf
Data publikacji:
2010-07
Wydawca:
Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:
87.64.kv
87.15.kp
Opis:
The application of fluorescence spectroscopy methods to determining the properties of analogues of camptothecin, promising anticancer agents, are described in this paper. The fluorescence anisotropy measurements provide useful information about the binding of camptothecin and its analogues to cell membranes and human serum albumin (HSA) that is important for potential clinical applications of these agents, and permit the selection from many camptothecin analogues those ones exhibiting desirable biomedical properties. Fluorescence anisotropy measurements prove that 3 new camptothecin analogues: 7-tert-butyldimethylsilyl-10-hydroxy-campthothecin, 7-trimethyl-silylethyl-10-hydroxy-camptothecin and 7-trimethyl-silyl-ethyl-10-amino-camptothecin exhibit high affinity of their lactone forms to membranes and low affinity of their carboxylate forms to HSA. Such properties should ensure high stability of these agents in physiological fluids, including blood.
Źródło:
Acta Physica Polonica A; 2010, 118, 1; 99-102
0587-4246
1898-794X
Pojawia się w:
Acta Physica Polonica A
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Determination of the Protein-Binding Properties of Camptothecins by Means of Optical Spectroscopy Methods
Autorzy:
Ziomkowska, B.
Cyrankiewicz, M.
Wybranowski, T.
Kruszewski, S.
Powiązania:
https://bibliotekanauki.pl/articles/1197530.pdf
Data publikacji:
2014-04
Wydawca:
Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:
87.64.K-
87.64.kv
87.15.kp
02.50.Sk
Opis:
Optical spectroscopy methods are widely used in studies of drugs. The affinity of camptothecins - anticancer agents - to human serum albumin (HSA) was determined in this work. Camptothecins (CPTs) exist in two forms: active lactone and open ring inactive carboxylate. In blood, the hydrolysis process of lactone form occurs which leads to deactivation of CPTs. Research is being done on biophysical properties of synthesized CPT compounds, in particular on binding to albumin. The affinity to plasma proteins is an important determinant of stability of CPTs in blood. The following analogues of CPT were tested in this paper: irinotecan, SN-38, topotecan, and 9-amino camptothecin. Using the method of fluorescence anisotropy measurement, the association constants of the studied compounds to HSA were determined. The authors attempted to determine the deactivation rate of topotecan in HSA solution using Principal Component Analysis and Factor Analysis of absorption spectra recorded during hydrolysis process of lactone form.
Źródło:
Acta Physica Polonica A; 2014, 125, 4A; A-61-A-65
0587-4246
1898-794X
Pojawia się w:
Acta Physica Polonica A
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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