A study on the binding interaction between the imidazole derivative and bovine serum albumin by fluorescence spectroscopy

Spectroscopic studies on interactions of the tetrakis(acetato)chloridodiruthenium(II,III) complex and the Ru2(II,III)-NSAID-derived metallodrugs of ibuprofen and ketoprofen with human serum albumin

“…Higher temperatures favor larger diffusion coefficients, thus increasing the bimolecular quenching constant in the dynamic process [114]. In addition, the diffusional limit in collisional quenching leads to k q maximum value of 2×10 10 mol -1 L s -1 [110]. [115], and different Ru(II) complexes (~10 4 mol -1 L) [101,[116][117][118].…”

Constrained Photophysics of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one in the Bioenvironment of Serum Albumins: A Spectroscopic Endeavour Supported by Molecular Docking Analysis

“…As many bioactive small molecules bind reversibly to serum albumins, it is important to study the interactions of drugs with this protein as these studies can provide information about the structural features that determine the therapeutic effect of drugs and have become an interesting research field in life science, chemistry and clinical medicine. The study regarding the mode of binding of various molecules to serum albumins is chiefly accountable for the understanding of metabolism, bio-distribution, elimination or pharmacological effects of the drugs in the body [5][6][7][8][9][10][11][12][14][15][16][17][18][19][20][21][22][23][24][25][26]. Knowledge of interaction mechanisms between endogenous and exogenous molecules and plasma proteins has a great value for researchers to understand the pharmacodynamics and pharmacokinetics of a drug candidate.…”

“…The lack of toxicity and immunogenicity make it an ideal candidate for drug delivery [13][14][15]. Hence, knowledge of binding with serum albumins is essential [16][17][18][19][20][21][22][23][24][25][26][27].…”

“…The dye has been used extensively for various photophysical applications as described elsewhere [49]. In scientific literature, there is no scarcity of examples of various fluorophore-BSA ⁄ HSA binding interactions [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28]. However, no other research group has ever thought of investigating such an important class (ketotetrahydrocarbazole based) of fluorophores with serum albumins.…”

Probing the binding of (+)-catechin to bovine serum albumin by isothermal titration calorimetry and spectroscopic techniques

“…Bovine serum albumin (BSA) has been one of the most extensively studied of this group of proteins, not only because of its medical importance, abundance, low cost, ease of purification, ready availability, unusual ligand-binding properties and it is widely accepted in the pharmaceutical industry http://dx.doi.org/10.1016/j.molstruc.2015.02.082 0022-2860/Ó 2015 Elsevier B.V. All rights reserved. [2][3][4], but also because of its structural homology with human serum albumin (HSA) [5,6]. The BSA molecule is made up of three homologous domains (I, II, III) that are divided into nine loops (L1-L9) by 17 disulfide bonds.…”