M. Maciążek-Jurczyk

TL;DR: It was concluded that colchicine may probably cause displacement of phenylbutazone from its complex with serum albumin (SA) and Static and dynamic quenching for the binary and ternary systems showed that phenyl butazone does not affect the complex formed between colchichine and BSA, and colchicaine has no effect on the Phe–BSA complex.

TL;DR: The conclusion that both Phe and MTX form a binding site in the same subdomain (IIA) points to the necessity of using a monitoring therapy owning to the possible increase of the uncontrolled toxic effects.

TL;DR: The main goal of the paper was to explain the possible alteration of human serum albumin binding properties induced by modifications such as glycation, oxidation and ageing.

TL;DR: Estimation of how non-enzymatic glycation of human serum albumin altered its tertiary structure using fluorescence technique found that the red-shift for gHSA(FRC) is higher than for HSA.

TL;DR: The main goal of the research was aggregation/fibrillation of HSA, the study of the physicochemical properties of formed amyloid fibrils using thioflavin T (ThT) and the analysis of ligand binding to aggregated/ fibrillated albumin in the presence of dansyl-l-glutamine, phenylbutazone and ketoprofen.