Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Ester

Abstract

Interactions of 2-[(carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic acid (compound

Structural Insights into the Ligand–LsrK Kinase Binding Mode: A Step Forward in the Discovery of Novel Antimicrobial Agents

“… where F 0 is the emission fluorescence of LsrK in the absence of ligands, F is the emission fluorescence of the protein in the presence of the ligand at the concentration [Q], f a is the fraction of accessible fluorophore to the ligands, and K SV is the Stern–Volmer constant. The analysis of the data using the modified Stern–Volmer equation is the classical model used in the interpretation of some results of fluorescence quenching in protein solution when the Stern–Volmer plot negatively deviates from linearity, [ 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 ] since it allows for investigating in detail the quenching mechanism that is occurring between ligands and proteins. Indeed, the linearity of the modified Stern–Volmer plots indicates static quenching (i.e., binding) in the presence of an inaccessible population of fluorophores and the plot allows for the calculation of the dissociation constant (K D ) and the percentage of fluorophores accessible to the quenchers.…”

Interaction of the nitrosyl ruthenium complex [RuII (NH.NHq‐R)(tpy)NO]3+ with human serum albumin: a spectroscopic and computational investigation

“…In HSA there is a single Trp residue (Trp‐214) located on the hydrophobic cavity of site I. [ 22 ] Fluorescence emission gave relevant information about changes in the Trp‐214 environment. [ 37 ] Additionally, individual RuBDQ–HSA solutions caused concentration‐dependent quenching of the intrinsic fluorescence of HSA (Figure S6) without changing the emission maximum and peak shape.…”