2 research outputs found
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. Moreover, conformational changes of protein upon binding with
SO and NR are provided by synchronous and circular dichroism (CD)
measurements. Molecular docking study provided the exact binding location
of SO and NR in lysozyme. Along with this study, molecular dynamics
simulation is carried out to measure the stability of Lyz, Lyz–SO,
and Lyz–NR complex. The present study revealed the strong binding
affinity of dyes with lysozyme, and this study would be helpful toward
medical and environmental science
Impact of imidazolium-based ionic liquids on the structure and stability of lysozyme
<p>Various types of water-miscible aprotic ionic liquids (ILs) with different cations (1-ethyl-3-methylimidazolium, 1-butyl-3-methylimidazolium, 1-octyl-3-methylimidazolium) and anions (ethylsulfate and chloride) were used as co-solvents to investigate the stability of lysozyme. Different techniques such as fluorescence, thermal absorption, and circular dichroism (CD) spectroscopy have been used for the study. Fluorescence results reveal that the addition of ILs (1-ethyl-3-methylimidazolium ethyl sulfate and 1-ethyl-3-methylimidazolium) increases the hydrophobicity around the tryptophan environment in lysozyme. CD analysis and temperature-dependent studies were done to investigate the stability of the protein. From the CD analysis, it was observed that the ILs keep the native structure of protein intact. Thermal denaturation studies depicted that the melting temperature of the protein increased in the presence of ILs (1-ethyl-3-methylimidazolium ethyl sulfate and 1-ethyl-3-methylimidazolium), which indicates the stabilization of the protein.</p