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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00121266" target="_blank" >RIV/00216224:14740/21:00121266 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1016/j.colsurfb.2021.111696" target="_blank" >https://doi.org/10.1016/j.colsurfb.2021.111696</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.colsurfb.2021.111696" target="_blank" >10.1016/j.colsurfb.2021.111696</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 β-sheet. The experimental findings were well supported by the molecular dynamics simulation results.

Název v anglickém jazyce

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

Popis výsledku anglicky

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 β-sheet. The experimental findings were well supported by the molecular dynamics simulation results.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Colloids and Surfaces B: Biointerfaces

ISSN

0927-7765

e-ISSN

1873-4367

Svazek periodika

202

Číslo periodika v rámci svazku

June

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

10

Strana od-do

111696

Kód UT WoS článku

000663336700004

EID výsledku v databázi Scopus

2-s2.0-85103327693