Unraveling the binding interactions between two Pt(II) complexes of aliphatic glycine derivatives with human serum albumin: A comprehensive computational and multi-spectral investigation.

This article delves into the interaction between HSA protein and synthesized platinum complexes, with formula: [Pt(Propyl-NH)(Propylglycine)]NO and [Pt(Tertpentyl-NH)(Tertpentylglycine)]NO, through a range of methods, including spectroscopic (UV-visible, fluorescence, synchronous fluorescence and CD) analysis and computational modeling (molecular docking and MD simulation). The binding constants, the number of binding sites, and thermodynamic parameters were obtained at 25 to 37 °C. The study found that both complexes could bind with HSA (moderate affinity for Tertpentyl and strong affinity for Propyl derivatives) and occupied one binding site in HSA (validated with, Stern-Volmer, Job-plots, and molecular docking investigations) located in subdomain IIA.

Molecular insights into the interaction of 5-fluorouracil and FeO nanoparticles with beta-casein: An experimental and theoretical study.

We investigated the potential carrier of milk beta-casein (β-CN) and its interactions with 5-fluorouracil (5-FU) and iron oxide nanoparticles (FeO NPs). We used different spectroscopic methods of fluorescence, UV-Visble, circular dichroism (CD), synchronous fluorescence, zeta potential assay, and computational studies to clarify the protein interaction with 5-FU and FeO NPs. The fluorescence data indicated both FeO NPs and 5-FU could quench the intrinsic fluorescence of β-CN.

Multi-spectroscopic studies of the interaction of new synthesized platin complex with human carrier protein of serum albumin.

Previous reports have shown that protein-drug interaction helps to improve the pharmacokinetics of the drugs. Human serum albumin (HSA) is one of the basic components of blood plasma and it serves as a storage and carrier protein. In the present study, the interaction of a new synthesized Pt [iso]2 complex (cis - [Pt(NH-Isopentylamine)(Isopentylglycine)]NO with HSA was studied using the spectroscopic methods of fluorescence and circular dichroic (CD) at two different temperatures of 25 and 37 °C.

Probing the interaction of two chemotherapeutic drugs of oxali-palladium and 5-fluorouracil simultaneously with milk carrier protein of β-lactoglobulin.

β-Lactoglobulin (βLG) is a basic element of globular carrier protein, which is the major protein in the whey of ruminant milk and is of main interest in the dairy industry. In the present study, the simultaneous effects of both of the important anticancer drugs of 5-fluorouracil (5-FU) and oxali-palladium, on the structure of βLG were investigated using different spectroscopic methods of fluorescence and circular dichroism (CD) in combination with a molecular docking at two temperatures of 25 and 37°C. The resulted data from intrinsic fluorescence spectra of protein indicated that 5-FU and oxalli-palladium can quench the fluorescence intensity of βLG in dose-dependent manner via static mechanism of fluorescence quenching.

Assay of bacteriorhodopsin stability on polycarbonate surface by using of FTIR-ATR: a model of disk-based bioassays.

Bacteriorhodopsin (BR) is a transmembrane protein which able to transport protons through cell membrane and thus converting solar energy to electrical energy. Up to now different strategies have been used to immobilize BR. In the present study the BR has been immobilized on polycarbonate surface with two different methods.