Molecular insights into binding mechanism of rutin to bovine serum albumin - Levothyroxine complex: Spectroscopic and molecular docking approaches.

Bovine serum albumin (BSA) has been used as a transporter protein for levothyroxine (LT4) and rutin, due to its property of binding to various ligands. Rutin binding to the BSA-LT4 complex can bring many benefits due to its proven pharmacological properties. Using Fourier-Transform Infrared Spectroscopy (FT-IR) the changes induced by rutin in the structure of BSA-LT4 complex were determined.

Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies.

Human serum transferrin (HST) is a glycoprotein involved in iron transport that may be a candidate for functionalized nanoparticles to bind and target cancer cells. In this study, the effects of the simple and doped with cobalt (Co) and copper (Cu) ferrihydrite nanoparticles (Fh-NPs, Cu-Fh-NPs, and Co-Fh-NPs) were studied by spectroscopic and molecular approaches. Fluorescence spectroscopy revealed a static quenching mechanism for all three types of Fh-NPs.

Probing the interaction of fisetin with human serum transferrin via spectroscopic and molecular docking approaches.

The binding of fisetin to human serum transferrin (HST) was investigated by spectroscopic (steady-state fluorescence, synchronous fluorescence, Förster resonance energy transfer) and molecular docking approaches. HST fluorescence is quenched by fisetin by a static process. The binding takes place with a moderate affinity and it is driven by hydrogen bonding and van der Waals forces.

Structural and molecular aspects of flavonoids as ligands for serum transferrin.

Human serum transferrin (HST) acts as a carrier for Fe and other ions. Binding of flavonoids to HST produces changes in the protein structure with direct implication on iron delivery into cells. We investigate the binding mechanism and affinity towards HST of three flavonoids: rutin, luteolin, and apigenin by different techniques: UV-Vis, fluorescence, fluorescence resonance energy transfer (FRET) combined with molecular docking.

Exploring the Conformation and Thermal Stability of Human Serum Albumin Corona of Ferrihydrite Nanoparticles.

In the last few years, a great amount of attention has been given to nanoparticles research due to their physicochemical properties that allow their use in analytical instruments or in promising imaging applications on biological systems. The use of ferrihydrite nanoparticles (Fh-NPs) in practical applications implies a particular control of their magnetic properties, stability, biocompatibility, interaction with the surface of the target, and low toxicity. In this study, the formation and organization of human serum albumin (HSA) molecules around the simple Fh-NPs and Fh-NPs doped with Co and Cu were examined by Scanning Electron Microscopy (SEM) and Atomic Force Microscopy (AFM) in terms of morphology and particle size.