Biophysical and molecular docking insight into the interaction of cytosine β-D arabinofuranoside with human serum albumin

A biophysical and computational study unraveling the molecular interaction mechanism of a new Janus kinase inhibitor Tofacitinib with bovine serum albumin

“…Fluorescence intensity measurement is a sensitive technique to examine the conformational and structural changes in proteins, because of alterations in the microenvironment around the fluorophores present in proteins. Notably, intrinsic fluorescence property of protein (BSA) is associated because of the presence of aromatic amino acid residues viz, Trp, Tyr, and Phe . Quenching in the fluorescence intensity occurs because of the interaction of drugs/ligands with the fluorophores present in the protein (BSA).…”

Biophysical insight into the anti-amyloidogenic behavior of taurine

“…HSA in reversibly and non-covalent manner interacts with diverse class of molecules within subdomain IB. Subdomain IB actively participates in binding with natural products (limonene, aristolochic acid, glycyrrhetinic acid) [47] and anticancer drugs and formulations (cytosine ␤-d arabinofuranoside, doxorubicin, camptothecin, daunorubicin, teniposide, suramin) [54]. Moreover, anticoagulant dicoumarol, steroids (bile acids, carbenoxolone), and synthetic dyes (azocarmine B, methyl orange), trans-feruloyl maslinic acid, 7-hydroxy-4-methyl coumarin derivatives and lidocaine strongly bind to the IB domain [55].…”

Interaction between quinoline yellow and human serum albumin: spectroscopic, chemometric and molecular docking studies

“…As shown in Fig. (B), two characteristic negative bands around 208 and 222 nm related to the α‐helical structure of protein were observed in the far‐UV CD spectrum of HSA . Compared with the CD spectrum of free HSA, the shape of the HSA CD spectra in the presence of QY did not change, suggesting that the α‐helical structure still played a predominant role in HSA conformation after binding of QY .…”