Study on the Interaction between Florasulam and Bovine Serum Albumin

Abstract

In this paper, the interaction between florasulam (FU, 2',6',8-trifluoro-5-methoxy [Kragh-Hansen U, Molecular aspects of ligand binding to serum albumin. Pharmacol Rev 33(1):17-53 1981; Carter DC and Ho JX, Structure of serum albumin. Adv Protein Chem 45:153-203 1994; He XM, and Carter DC, Atomic structure and chemistry of human serum albumin. Nature 358(6383):209-215 1992] triazolo [1,5-c]pyrimidine-2-sulfonanilide) and bovine serum albumin (BSA) was investigated by fluorescence, ultraviolet absorption (UV) and Far-UV circular dichroism (CD) spectrometries. A strong fluorescence quenching was observed and the quenching mechanism was considered as static quenching. The binding constant of FU with BSA at 299 and 309 K were obtained as 1.5 x 10(4) and 7.1 x 10(3) l mol(-1), respectively. There was one binding site between FU and BSA. The thermodynamic parameters enthalpy change (DeltaH) and entropy change (DeltaS) were calculated as -57.89 kJ mol(-1) and -113.6 J mol(-1) K(-1), respectively, which indicated that the acting force between FU and BSA was mainly hydrogen bond and Van der Waals force. According to the Förster non-radiation energy transfer theory, the average binding distance between donor (BSA) and acceptor (FU) was obtained (r = 1.59 nm). The investigations of the UV/Vis and CD spectra of the system showed that the conformation of BSA was changed in presence of FU.

Investigation of the interaction of anthraquinones of Cassia occidentalis seeds with bovine serum albumin by molecular docking and spectroscopic analysis: Correlation to their in vitro cytotoxic potential

“…) in the body are often correlated with their affinity toward serum albumin. Hence, the study of such molecules with respect to albumin binding has fundamental importance in relation to retention in the body (Tian et al, 2003;Ran et al, 2007). Since AQs were detected in the serum of hepatomyoencephalopathy patients as well as in rats fed with CO seeds (Panigrahi et al, 2015), it is pertinent to study the interaction of these AQs with albumin.…”

Interaction between felodipine and bovine serum albumin: fluorescence quenching study

“…Although various researchers have studied the structure and properties of serum albumin and its interaction with small molecules such as dyes, drugs and toxic chemicals using the FRET process, [8][9][10][11][12][13][14] there has been no report on the drug-protein interaction, especially FLD and BSA. In this regards, in the present work, we made a detailed and insightful study on the interaction between FLD and BSA by using nondestructive FRET spectroscopy.…”

Versatility of 7-Substituted Coumarin Molecules as Antimycobacterial Agents, Neuronal Enzyme Inhibitors and Neuroprotective Agents

“…warfarin) are known to bind extensively to blood-soluble proteins. Serum albumins, which are the major soluble protein constituents of the circulatory system (4% w/v), have the ability to reversibly bind a large variety of exogenous compounds including fatty acids, amino acids, drugs and pharmaceuticals [34][35][36]. Plasma protein binding forms an integral part of distribution and bioavailability for numerous medications currently on the market but might also become problematic where binding is extensive [37,38].…”