Interaction of mitoxantrone with human serum albumin: Spectroscopic and molecular modeling studies

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

“…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.…”

“…Serum albumins, widely studied transport proteins are abundantly found in blood plasma [1][2][3][4][5][6][7][8][9][10][11][12]. Besides being an attractive macromolecular carrier, serum albumins play a vital role by increasing the solubility of hydrophobic drugs in the blood plasma, binding with bio-active molecules and maintaining colloid blood pressure [3,4].…”

“…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.…”

A Study of the Interaction Betweentrans-Dehydrocrotonin, a Bioactive Natural 19-nor-Clerodane, and Serum Albumin

“…These data indicate a moderate change in the secondary structure of BSA, but the structure of albumin remains predominantly as α-helix. 47 This decrease on the intensity of these two absorptions is probably occurring due to the high kinetic volume of the diterpene.…”

Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy

“…Of the three aromatic amino acid residues, tryptophan (Trp) contributes most to intrinsic protein fluorescence [28]. The effect of PDQL on the fluorescence emission spectra of HSA was first tested (Figure 2 Fluorescence quenching could proceed via dynamic or static quenching or a combination of both [29,30]. Dynamic quenching involves the collisional encounters between the quencher and the fluorophore during the lifetime of the excited state, whereas static quenching involves the formation of a ground state complex between the fluorophore and the quencher [31].…”