Informace o publikaci

Polyethylene glycol perturbs the unfolding of CRABP I: A correlation between experimental and theoretical approach

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SUBADINI Suchismita BERA Krishnendu HRITZ Jozef SAHOO Harekrushna

Rok publikování 2021
Druh Článek v odborném periodiku
Časopis / Zdroj Colloids and Surfaces B: Biointerfaces
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://doi.org/10.1016/j.colsurfb.2021.111696
Doi http://dx.doi.org/10.1016/j.colsurfb.2021.111696
Klíčová slova PEG; protein stabilizer; Crowding agent; excluded volume; protein unfolding
Popis 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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