A fluorescent reporter detects details of aromatic ligand interference in drug-binding sites of human serum albumin

Serum Albumin Conformational Disturbances in Melancholic Depression can be Revealed Using Time Resolved Tryptophan Fluorescence

“…In HAS excitation at >295 nm is absorbed mainly by tryptophan 214 (Trp-214) residues thus excitation in the range of 295 -305nm permits to observe the state of its environment. For the formal description of the kinetics of fluorescent decay of tryptophan it is necessary to use the sum of not less of 3 exponentials [7]: Analysis of all fluorescence decay parameters of Trp-214-R in the serum samples of controls and patients before the treatment showed that the mean amplitudes A1 and A3 in the serum of these patients were significantly lower than in the group of controls. The application of the Wilcoxon test to independent samples of controls and patients showed a significant difference (p=0.01) between these groups: for A1 -440±16v 378±5 and A3 -327±15v 285±7, respectively (for A2 -p=0.1).…”

Albumin Retains Its Transport Function after Interaction with Cerium Dioxide Nanoparticles

“…Moreover, the affinity of K-35 to the albumin-binding sites is comparable to the affinity of the most well-characterized HSA-binding drugs (e.g., warfarin and ibuprofen). 115 The K-35 probe was shown to act as an effective general marker of transport property of HSA, and it was successfully used to trace the changes in the albumin-binding capacity in various models of pathological processes. 115,118 The changes in albumin-bound CAPIDAN fluorescence were shown to be even a better marker of the severity and prognosis of human pathological states than the results of commonly accepted laboratory tests.…”

“…115−117 The K-35 fluorescent probe is advantageous due to the high selectivity and specificity of albumin binding, high sensitivity and applicability for the analysis of biological fluids with a low protein content, as well as its nondestructive properties. 115,117 Upon interaction with HSA, K-35 molecules occupy the binding sites of four types. 115,117,118 90−95% of K-35 fluorescence in blood plasma is due to its binding to albumin.…”

“…115,117 Upon interaction with HSA, K-35 molecules occupy the binding sites of four types. 115,117,118 90−95% of K-35 fluorescence in blood plasma is due to its binding to albumin. 115−117 If any of the sites lose their binding capacity, the amount of K-35 capable of interaction with HSA decreases, which results in the decrease in the intensity of the characteristic fluorescence.…”

“…115 The K-35 probe was shown to act as an effective general marker of transport property of HSA, and it was successfully used to trace the changes in the albumin-binding capacity in various models of pathological processes. 115,118 The changes in albumin-bound CAPIDAN fluorescence were shown to be even a better marker of the severity and prognosis of human pathological states than the results of commonly accepted laboratory tests. 115,117 To study the effect of CeO 2 NPs on the transport properties of albumin, a K-35 fluorescent probe (4-(dimethylamino)naphthalic acid N-(carboxyphenyl)imide) was used, which allowed the selective monitoring of changes in protein drug centers by Trp fluorescence.…”