Nonenzymatically glycated human serum albumin and glycated poly-lysine(Lys) in vitro brought about the reduction of nitroblue tetrazolium and ferricytochrome c at pH 9.06 and pH 7.8, respectively. This reduction was inhibited partially by superoxide dismutase (SOD). Glycated poly-Lys caused the oxidation of NADH in the presence of LDH at pH 7.0 which was completely inhibited by SOD. Glycated material was found to function both as a reductant and an oxidant. The reactivity of glycated material is discussed and a possible mechanism by which superoxide is produced is proposed. Results may give a clue to diabetic complications.

Superoxide production from nonenzymatically glycated protein

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

The role of polymer size and hydrophobic end-group in PEG-protein interaction.

In this report, we have investigated the binding affinity of tofacitinib with human serum albumin (HSA) under simulated physiological conditions by using UV-visible spectroscopy, fluorescence quenching measurements, dynamic light scattering (DLS), differential scanning calorimetry (DSC) and molecular docking methods. The obtained results demonstrate that fluorescence intensity of HSA gets quenched by tofacitinib and quenching occurs in static manner. Binding parameters calculated from modified Stern-Volmer equation shows that the drug binds to HSA with a binding constant in the order of 10(5). Synchronous fluorescence data deciphered the change in the microenvironment of tryptophan residue in HSA. UV spectroscopy and DLS measurements deciphered complex formation and reduction in hydrodynamic radii of the protein, respectively. Further DSC results show that tofacitinib increases the thermo stability of HSA. Hydrogen bonding and hydrophobic interaction are the main binding forces between HSA and tofacitinib as revealed by docking results.

Binding of Janus kinase inhibitor tofacitinib with human serum albumin: multi-technique approach

The binding interaction between temsirolimus, an important antirenal cancer drug, and HSA, an important carrier protein was scrutinized making use of UV and fluorescence spectroscopy. Hyper chromat...

Probing the interaction of anticancer drug temsirolimus with human serum albumin: molecular docking and spectroscopic insight.

The interaction between metformin and human serum albumin (HSA), as well as its glycated form (gHSA) was investigated by multiple spectroscopic techniques, zeta potential, and molecular modeling under physiological conditions. The steady state and time-resolved fluorescence data displayed the quenching mechanism of HSA-metformin and gHSA-metformin was static. The binding information, including the binding constants, number of binding sites, effective quenching constant showed that the binding affinity of metformin to HSA was greater than to gHSA which also confirmed by anisotropy measurements. It was determined that metformin had two and one set of binding sites on HSA and gHSA, respectively. Far-UV CD spectra of proteins demonstrated that the α-helical content decreased with increasing metformin concentration. The zeta potential and resonance light scattering (RLS) diagrams provided that lower drug concentration induced metformin aggregation on gHSA surface as compare to HSA. The increase in polarizability was one of the important factors for the enhancement of RLS and the formation of drug/protein complexes. The zeta potential results suggested that both hydrophobic and electrostatic interactions played important roles in the protein-metformin complex formation. Site marker experiments and molecular modeling showed that the metformin bound to subdomain IIIA (Sudlow's site II) on HSA and gHSA.

Binding site identification of metformin to human serum albumin and glycated human serum albumin by spectroscopic and molecular modeling techniques: a comparison study.

Maryam Mahmoodian-Moghaddam

Papers

Binding site identification of metformin to human serum albumin and glycated human serum albumin by spectroscopic and molecular modeling techniques: a comparison study.