2007
DOI: 10.1002/cbdv.200790227
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Spectroscopic Analysis of the Binding Interaction Between Tinidazole and Bovine Serum Albumin (BSA)

Abstract: The interaction between bovine serum albumin (BSA) and tinidazole (Tindamax; 1) in aqueous solution was investigated in detail by means of UV/VIS and fluorescence spectroscopy, as well as through resonance light-scattering (RLS) spectroscopy. The apparent binding constant and number of binding sites were determined at three different temperatures, as well as the average binding distances between 1 and the nearest amino acid residue(s) of BSA, as analyzed by means of Förster's theory of non-radiation energy tra… Show more

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Cited by 12 publications
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“…Fluorescence quenching can be distinguished by its dependence on temperature and excited state life time. Higher temperatures will result in a faster diffusion and an increased collisional quenching . Thus the quenching constant values will increase when the temperature is increased.…”
Section: Resultsmentioning
confidence: 99%
“…Fluorescence quenching can be distinguished by its dependence on temperature and excited state life time. Higher temperatures will result in a faster diffusion and an increased collisional quenching . Thus the quenching constant values will increase when the temperature is increased.…”
Section: Resultsmentioning
confidence: 99%