Fluorescence Studies of Anti-Cancer Drugs - Analytical and Biomedical Applications

Abstract

The fluorescence properties of anticancer drugs (ACDs), including steady-state native fluorescence, time-resolved fluorescence, fluorescence polarization, excimer and exciplex emission, laser-induced fluorescence (LIF) with one- or two-photon excitation are reviewed, as well as the use of fluorogenic labels and fluorescent probes for the non-fluorescent ACDs. The interest of monitoring the fluorescence spectral changes to study the interactions of ACDs with biomolecules, such as DNA, proteins, vesicles, and the formation of complexes is discussed. The fluorescence methodologies used for ACDs studies, including fluorescence with two-photon excitation, liquid chromatography and capillary electrophoresis with fluorescence and laser-induced fluorescence (LIF) detection, and fluorescence microscopy, are also surveyed. Analytical and bioanalytical applications of fluorescence, indicating good selectivity and very low limits of detection at the nanomolar and picomolar level for most ACDs, are described. Biomedical and clinical applications of the fluorescence methods, mostly oriented towards the evaluation of the cytoxicity and anti-tumor potential of ACDs in single cells as well as in biological fluids, including blood, serum, plasma, cerebrospinal fluid, urine and feces, are also discussed in detail. This review is based on selected literature published in the last decade (1994-2003).

Capillary electrophoresis of proteins 2005–2007

“…The use of various analytical methods for drug-protein binding measurements has been reviewed [152,153]. Recently CE has been used to measure binding of anticancer gallium(III) complexes to transferrin and serum albumin [154], novel antitumor ruthenium(III) complexes to human serum proteins [155][156][157], anticancer drugs to serum proteins [158], basic drugs to serum proteins, BSA, and a 1 -acid glyco-protein [159], theophylline to human serum albumin [160], oxindole alkaloid from Uncaria tomentosa to amyloid protein for potential treatment of Alzheimer's disease [161], new propranolol analogues to serum proteins [162], a dimeric inhibitor to 3C-like proteinase [163], roscovitine to plasma proteins [164], and drug suramin to b 2 -microglobulin [165,166]. The effect of drug complexation on stability and conformation of human serum albumin has been also studied [167].…”

Open‐ITC: an alternate computational approach to analyze the isothermal titration calorimetry data of complex binding mechanisms

“…The interaction of a protein with a ligand or another protein plays an integral role in its function. To assess and quantify the intramolecular or intermolecular interactions, techniques such as isothermal titration calorimetry (ITC) (Ladbury, ), fluorescence polarization (Aaron and Trajkovska, ), surface plasmon resonance (McDonnell, ), nuclear magnetic resonance (NMR) (Fejzo et al ., ), and so on are commonly used. ITC is one of the techniques that measure the heat released/absorbed during the interaction process, which contains finer details of the binding mechanism.…”

Liquid chromatographic analysis of the anticancer alkaloid luotonin A and some new derivatives in human serum samples

“…This property makes it possible to use FL measurements with analytical and biomedical purposes [8]. The studies of cytotoxicity and selectivity of the new antitumor agents in tumor cells require sensitive and selective analytical methods.…”

“…The studies of cytotoxicity and selectivity of the new antitumor agents in tumor cells require sensitive and selective analytical methods. Several HPLC procedures have been described for the determination of camptothecin [8][9][10][11][12][13][14][15][16][17][18][19][20], including the isocratic elution of camptothecin and its analogs using ACN/phosphate buffer as the mobile phase [13]. Isocratic and gradient separations coupled to UV-Vis [14,15] Víctor Gonzá lez-Ruiz and diode array detection [16] have been employed successfully.…”