The effect of putrescine on the lysozyme activity and structure: Spectroscopic approaches and molecular dynamic simulation.

The present research addressed the influence of polyamine (putrescine) on the compound as well as function of lysozyme; accordingly, UV- Visible, fluorescence spectroscopy and simulation method were applied to fulfill this goal. Lysozyme's structural variability was examined at various putrescine ‌concentrations; also, the putrescine binding to lysozyme was addressed using spectrofluorescence, circular dichroism (CD) and UV-Vis measurements. The obtained results indicated that with raising the putrescine concentration, the intrinsic quenching fluorescence of lysozyme was decreased based on the static mechanism.

A comparative study of the interaction of naringenin with lysozyme by multi-spectroscopic methods, activity comparisons, and molecular modeling procedures.

The present study applied steady-state fluorescence, UV-Vis spectrophotometry, molecular docking studies, and circular dichroism (CD) to investigate the interaction of naringenin with lysozyme in an aqueous medium. The UV-Vis measurement indicated the changes in lysozyme secondary and tertiary structure change as a function of the concentration of naringenin. Naringenin could be used to turn the static quenching mechanism into the intrinsic fluorescence of lysozyme.

Characterization of osmolyte-enzyme interactions using different spectroscopy and molecular dynamic techniques: Binding of sucrose to proteinase K.

Osmolytes such as sucrose can interact with the proteins. The aim of the present investigation was to characterize how sucrose could affect the structure, thermal stability and the kinetic of proteinase K. UV-vis spectroscopy, fluorescence spectroscopy, circular dichroism, molecular docking, molecular dynamic simulation studies were used to this end.

Comparative studies on the interaction between biogenic polyamines and bovine intestinal alkaline phosphatases: spectroscopic and theoretical approaches.

In this work, the effect of two organic polyamines (spermine and spermidine) on the fluorescence intensity and activity of bovine intestinal alkaline phosphatase (BIALP) are investigated. The interaction of BIALP with spermine and spermidine was studied in a diethanolamine buffer with 0.5 mM magnesium chloride (pH 9.

Catalytic activity, structure and stability of proteinase K in the presence of biosynthesized CuO nanoparticles.

Here, CuO nanoparticles were synthesized using Sambucus nigra (elderberry) fruit extract. Further, the binding of proteinase K, as a model enzyme with green synthesized nanoparticles was investigated. The results demonstrated that the structural changes in enzyme were induced by the binding of nanoparticles.

Conjugation of biogenic polyamine (putrescine) with proteinase K: Spectroscopic and theoretical insights.

To understand the influence of polyamine on conformation, stabilization and function of proteins, we used multispectroscopic and simulation methods through structural, stability and kinetic measurements of proteinase K (PK) as a model enzyme combined with putrescine (Put). Structural variability of PK was investigated at different concentrations of Put, using circular dichroism, spectrofluorescence and UV-vis measurements. The secondary structure of PK was changed through β-sheet to α-helix switch induced by Put.

Molecular investigation on the interaction of spermine with proteinase K by multispectroscopic techniques and molecular simulation studies.

The alteration in structure, function and stability of proteinase K in the presence of spermine was investigated using spectroscopic methods and simulation techniques. The stability and enzyme activity of proteinase K-spermine complex were significantly enhanced as compared to that of the pure enzyme. The increase in the value of V and the catalytic efficiency of Proteinase K in presence of spermine confirmed that the polyamine could bring the enzyme hyperactivation.