Publication details
Polyethylene glycol perturbs the unfolding of CRABP I: A correlation between experimental and theoretical approach
| Authors | |
|---|---|
| Year of publication | 2021 |
| Type | Article in Periodical |
| Magazine / Source | Colloids and Surfaces B: Biointerfaces |
| MU Faculty or unit | |
| Citation | |
| web | https://doi.org/10.1016/j.colsurfb.2021.111696 |
| Doi | http://dx.doi.org/10.1016/j.colsurfb.2021.111696 |
| Keywords | PEG; protein stabilizer; Crowding agent; excluded volume; protein unfolding |
| Description | The importance of macromolecules paves the way towards a detailed molecular level investigation as all most all cellular processes occurring at the interior of cells in the form of proteins, enzymes, and other biological molecules are significantly affected because of their crowding. Thus, exploring the role of crowding environment on the denaturation and renaturation kinetics of protein molecules is of great importance. Here, we have employed CRABP I (cellular retinoic acid binding protein I), as a model protein along with different molecular weights of Polyethylene glycol (PEG) as molecular crowders. The experimental evaluations were done by accessing the protein secondary structure analysis using circular dichroism (CD) spectroscopy and unfolding kinetics using intrinsic fluorescence of CRABP I at 37?°C to mimic the in vivo crowding environment. The unfolding kinetics results indicated that both PEG 2000 and PEG 4000 act as stabilizers by retarding the unfolding kinetic rates. Both kinetic and stability outcomes presented the importance of crowding environment on stability and kinetics of CRABP I. The molecular dynamics (MD) studies revealed that thirteen PEG 2000 molecules assembled during the 500?ns simulation, which increases the stability and percentage of ß-sheet. The experimental findings were well supported by the molecular dynamics simulation results. |
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