Abstract
The interaction between felodipine and bovine serum protein was studied, the optimal experimental conditions were selected, and the fluorescence quenching mechanism was discussed. The interaction between filodipine and bovine serum protein was determined by UV spectrophotometry, and the optimal experimental conditions were selected by control variable method. The mechanism of fluorescence quenching in the system was explored by fluorescence spectrophotometry. The fluorescence intensity of the system between felodipine and bovine serum protein was the most obvious under the experimental conditions of buffer solution pH 7.4, felodipine concentration 8.0*10-4mol/L, reaction time 30min and 25°C. Static fluorescence quenching caused by the formation of complex compounds.
Highlights
At present, the main drugs used for the treatment of hypertension include the following categories: diuretics, β-blockers, and calcium inhibitors [1,2,3,4]
The blank solvent had no obvious effect on the main absorption peaks of fluorescence intensity, the determination of felodipine standard solution is not affected by impurities
It can be seen that With the increase of felodipine concentration, the absorbance of the system increased continuously and presents a blue shift. This indicates that felodipine interacts with BSA, making tyrosine and tryptophan inside the protein exposed in a large number of polar solvents, and strengthening the absorption peak of the system
Summary
The main drugs used for the treatment of hypertension include the following categories: diuretics, β-blockers, and calcium inhibitors [1,2,3,4]. Its antihypertensive effect is mild and lasting, effective for a long time, and it is not easy to produce drug resistance. These drugs can be used independently to treat various types of hypertension. Used drugs mainly include nifedipine and felodipine [6], which are suitable for patients with coronary heart disease or peripheral vascular disease. It has a good effect on hypertension in the elderly. The reversible binding reaction between hormone and albumin can achieve a relatively stable albumin concentration [10,11,12]
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