Probing the interaction between niobium pentoxide nanoparticles and serum albumin proteins by Spectroscopic approaches.

Nanoparticles (NPs) can directly or indirectly enter into the body because of their small size; then they tend to alter the conformation and function of proteins upon interaction with them. Thus, it is crucial to understand the impact of NPs in a biological medium. Recently, niobium pentoxide nanoparticles (NbO NPs) are finding increasing applications in the biological system, for example, bone tissue and dental material, matrix for biosensing of proteins, .

Insights into the binding interaction between copper ferrite nanoparticles and bovine serum albumin: An effect on protein conformation and activity.

The binding affinity between bovine serum albumin (BSA) and copper ferrite (CuFe O ) nanoparticles in terms of conformation, stability and activity of protein was studied using various spectroscopic methods. The quenching involved in BSA-CuFe O NP interaction was static quenching as analysed by different techniques (steady-state and time-resolved fluorescence along with temperature-dependent fluorescence measurements). Among all types of possible interactions, it was revealed that the major binding forces were van der Waals interaction and hydrogen bonding, which were explored from negative values of enthalpy change (∆H = -193.

Exploring the effect of 5-Fluorouracil on conformation, stability and activity of lysozyme by combined approach of spectroscopic and theoretical studies.

In this present work, a detailed investigation of the effect of an anticancer drug, 5-Fluorouracil (5-FU), on conformation, stability and activity of lysozyme (Lyz) was reported. The interaction between Lyz and 5-FU was reflected in terms of intrinsic fluorescence quenching and change in secondary structure of Lyz. The mode of quenching mechanism involved was evaluated by the steady-state and time-resolved fluorescence measurements.

Molecular level insight into the effect of triethyloctylammonium bromide on the structure, thermal stability, and activity of Bovine serum albumin.

Understanding the interactions between protein and ionic liquids (IL) is vital in order to avail the ILs in biological applications. In this study, we have investigated the influence of triethyloctylammonium bromide on the structure, stability, and activity of Bovine Serum Albumin (BSA) using different spectroscopic methods Fluorescence and circular dichroism measurements revealed that BSA appears to be in a non-native compact structure in the presence of IL (up to concentration 0.02M).

A Spectroscopic and Molecular Simulation Approach toward the Binding Affinity between Lysozyme and Phenazinium Dyes: An Effect on Protein Conformation.

A comparative study of binding interaction between Safranin O (SO) and Neutral Red (NR) with lysozyme (Lyz) has been reported using several spectroscopic methods along with computational approaches. Steady-state fluorescence measurements revealed static quenching as the major quenching mechanism in Lyz-SO and Lyz-NR interaction, which is further supported by time-resolved fluorescence and UV-vis measurements. Additionally, binding and thermodynamic parameters of these interactions are calculated from temperature dependent fluorescence data.

Spectroscopic insight into the interaction of bovine serum albumin with imidazolium-based ionic liquids in aqueous solution.

The study of protein-ionic liquid interactions is very important because of the widespread use of ionic liquids as protein stabilizer in the recent years. In this work, the interaction of bovine serum albumin (BSA) with different imidazolium-based ionic liquids (ILs) such as [1-ethyl-3-methyl-imidazolium ethyl sulfate (EmimESO ), 1-ethyl-3-methyl-imidazolium chloride (EmimCl) and 1-butyl-3-methyl-imidazolium chloride (BmimCl)] has been investigated using different spectroscopic techniques. The intrinsic fluorescence of BSA is quenched by ILs by the dynamic mechanism.

Interaction of Lysozyme with Rhodamine B: A combined analysis of spectroscopic & molecular docking.

The interaction of Rhodamine B (RB) with Lysozyme (Lys) was investigated by different optical spectroscopic techniques such as absorption, fluorescence, and circular-dichroism (CD), along with molecular docking studies. The fluorescence results (including steady-state and time-resolved mode) revealed that the addition of RB effectively causes strong quenching of intrinsic fluorescence in Lysozyme and mostly, by the static quenching mechanism. Different binding and thermodynamic parameters were calculated at different temperatures and the binding constant value was found to be 2963.