Spectroscopic analyses and studies on respective interaction of cyanuric acid and uric acid with bovine serum albumin and melamine

Underlying the Mechanism of 5-Fluorouracil and Human Serum Albumin Interaction: A Biophysical Study

“…Where K 2 is the spatial orientation factor of the dipole, n is the refractive index of the medium, F is the fluorescence quantum yield of the donor, and J is the overlap integral of the fluorescence emission spectrum of the donor with the absorption spectrum of the acceptor, which can be calculated by the interaction of drug (5FU) with HSA induced some changes in the microenvironment and the confirmation of protein [19].…”

“…The interaction of 5FU with HSA was also characterized by studying the fluorescence anisotropy. Fluorescence anisotropy was measured for 5-FU with HSA of concentration ranging from 1-60 μM and the fluorescence anisotropy, r, was measured as follows: [19] r=(I VV -GI VH )/(I VV +2GI VH ) [3] Where, I VV and I VH were the intensities obtained by fixing the excitation polarizer orientation vertically and changing the emission polarizer orientation vertically and horizontally, respectively.…”

Graphitic carbon nitrides modified hollow fiber solid phase microextraction for extraction and determination of uric acid in urine and serum coupled with gas chromatography-mass spectrometry

“…1), is the final product of the purine metabolism and its abnormal levels in the body can affect renal function and blood pressure [1]. An elevated UA in urine or serum is associated with gout, hypertension, cardiovascular diseases, renal disease and Lesch-Nyhan syndrome [2,3], which is related to poor solubility of UA in water, strong interaction between UA and protein molecules [4] and complex redox-dependent pathways in vivo [5]. Therefore, establishing a simple, direct and accurate technique to monitor UA in biofluid is of great importance for diagnosing diseases and clinical study.…”

Spectroscopic and molecular modcking analysis of the interaction between Trypsin and Cefpirome

“…In addition, the synchronous fluorescence spectroscopy can confirm the specific binding site of drug to protein. For comparison, the synchronous fluorescence quenching ratios (R SFQ ) that express the decreasing percentages of synchronous fluorescence intensity were calculated by using the equation: [24] . The corresponding ratios of synchronous fluorescence quenching (R SFQ ) were illustrated in Figure 6.…”