Unveiling the binding details and esterase-like activity effect of methyl yellow on human serum albumin: spectroscopic and simulation study

Abstract

Details of the interaction between MY and HSA.

Multispectroscopic and Theoretical Investigation on the Binding Interaction of a Neurodegenerative Drug, Lobeline with Human Serum Albumin: Perturbation in Protein Conformation and Hydrophobic–Hydrophilic Surface

“…The reduction in emission intensity of a fluorophore on introducing a ligand can be categorized as either collisional, static, or a combination of static and dynamic quenching. ,, For intrinsic protein fluorescence, the Stern–Volmer equation is commonly used to interpret the fluorescence quenching process F 0 F = 1 + k q τ o false[ normalQ false] = 1 + K SV false[ normalQ false] The equation illustrates the relationship between protein emission intensities without a quencher ( F 0 ) and with a quencher ( F ), where the quencher [Q] in this context is the LOB.…”

“…Lifetime fluorescence decay measurements are instrumental in providing valuable information into the molecular environment and excited-state complex formation between proteins and ligands. , The fluorescence decay profiles of the protein, recorded with nanosecond resolution, were observed in the presence of the quencher (LOB), as shown in Figure b. The decay curves were analyzed using biexponential iterative fitting The given formula determined the average fluorescence lifetime (s) , : false⟨ τ false⟩ = τ 1 α 1 + τ 2 α 2 α i and τ i are the relative intensity and delay time for the i th fitting, respectively. The average fluorescence lifetime, “τ” is the sum of each delay time multiplied by its relative intensity.…”

“…CD is an expeditious and effective technique used in protein–ligand interaction studies to analyze the secondary structure of proteins and detect alterations in protein conformation upon ligand binding . The spectra in Figure a for HSA exhibit two negative bands, one at 208, which corresponds to the π–π* transition, and one at 222 nm, because of the transitions of n → π* peptide bonds. , These transitions are indicative of the α-helical structure of the HSA …”

“…The reduction in emission intensity of a fluorophore on introducing a ligand can be categorized as either collisional, static, or a combination of static and dynamic quenching. 29,17,33 For intrinsic protein fluorescence, the Stern−Volmer equation is commonly used to interpret the fluorescence quenching process. 34…”

“…33,38 The fluorescence decay profiles of the protein, recorded with nanosecond resolution, were observed in the presence of the quencher (LOB), as shown in Figure 2b. The decay curves were analyzed using biexponential iterative fitting 39 The given formula determined the average fluorescence lifetime (s) 17,30 :…”