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.
Systematic experimental investigation of MnO2–BSA complexes in terms of the structure and stability of the protein as well as the aggregation of the nanoparticle.
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 (EmimESO4), 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. The thermodynamic analysis demonstrates that very weak interactions exist between BSA and ILs. 8‐Anilino‐1‐naphthalenesulfonic acid (ANS) fluorescence and lifetime measurements reveal the formation of the compact structure of BSA in IL medium. The conformational changes of BSA were monitored by CD analysis. Temperature‐dependent ultraviolet (UV) measurements were done to study the thermal stability of BSA. The thermal stability of BSA in the presence of ILs follows the trend EmimESO4 > EmimCl > BmimCl and in the presence of more hydrophobic IL, destabilization increases rapidly as a function of concentration.
Amyloid fibrillogenesis of proteins is known to be the root cause of a large number of diseases like Parkinson's, Alzheimer's, and Huntington's disease, spongiform encephalopathy, amyloid polyneuropathy, type-II diabetes, etc.
The present study has been undertaken with an objective
to find
out a suitable medium for the long-term stability and storage of the ct-DNA structure in aqueous solution. For this purpose,
the potential of a pyrrolidinium-based dicationic ionic liquid (DIL)
in stabilizing ct-DNA structure has been investigated
by following the DNA–DIL interaction. Additionally, in order
to understand the fundamental aspects regarding the DNA–DIL
interaction in a comprehensive manner, studies are also done by employing
structurally similar monocationic ionic liquids (MILs). The investigations
have been carried out both at ensemble-average and single molecular
level by using various spectroscopic techniques. The molecular docking
study has also been performed to throw more light into the experimental
observations. The combined steady-state and time-resolved fluorescence,
fluorescence correlation spectroscopy, and circular dichroism measurements
have demonstrated that DILs can effectively be used as better storage
media for ct-DNA as compared to MILs. Investigations
have also shown that the extra electrostatic interaction between the
cationic head group of DIL and the phosphate backbone of DNA is primarily
responsible for providing better stabilization to ct-DNA, retaining its native structure in aqueous medium. The outcomes
of the present study are also expected to provide valuable insights
in designing new polycationic IL systems that can be used in nucleic
acid-based applications.
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