Determination of the Protein-Binding Properties of Camptothecins by Means of Optical Spectroscopy Methods |
| B. Ziomkowska, M. Cyrankiewicz, T. Wybranowski and S. Kruszewski
Medical Physics Division, Biophysics Department, Collegium Medicum of Nicolaus Copernicus University, JagielloĊska 13, 85-067 Bydgoszcz, Poland |
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| 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. |
DOI: 10.12693/APhysPolA.125.A-61 PACS numbers: 87.64.K-, 87.64.kv, 87.15.kp, 02.50.Sk |