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

J 2021

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

SUBADINI, Suchismita, Krishnendu BERA, Jozef HRITZ a Harekrushna SAHOO

Základní údaje

Originální název

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

Autoři

SUBADINI, Suchismita, Krishnendu BERA (356 Indie, domácí), Jozef HRITZ (703 Slovensko, garant, domácí) a Harekrushna SAHOO

Vydání

Colloids and Surfaces B: Biointerfaces, Elsevier, 2021, 0927-7765

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 5.999

Kód RIV

RIV/00216224:14740/21:00121266

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.colsurfb.2021.111696

UT WoS

000663336700004

Klíčová slova anglicky

PEG; protein stabilizer; Crowding agent; excluded volume; protein unfolding

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 30. 1. 2024 09:45, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

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.

Návaznosti

EF16_013/0001776, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii pro lidské zdraví

LM2018140, projekt VaV

Název: e-Infrastruktura CZ (Akronym: e-INFRA CZ)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, e-Infrastruktura CZ

LTAUSA18168, projekt VaV

Název: Selektivní NMR značení jako nástroj pro charakterizaci proteinových komplexů zapojených do neurodegenerativních onemocnění

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Selektivní NMR značení jako nástroj pro charakterizaci proteinových komplexů zapojených do neurodegenerativních onemocnění, INTER-ACTION

Citovat

SUBADINI, Suchismita, Krishnendu BERA, Jozef HRITZ a Harekrushna SAHOO. Polyethylene glycol perturbs the unfolding of CRABP I: A correlation between experimental and theoretical approach. Colloids and Surfaces B: Biointerfaces. Elsevier, 2021, roč. 202, June, s. 111696-111705. ISSN 0927-7765. Dostupné z: https://dx.doi.org/10.1016/j.colsurfb.2021.111696.

@article{1753483,
   author = {Subadini, Suchismita and Bera, Krishnendu and Hritz, Jozef and Sahoo, Harekrushna},
   article_number = {June},
   doi = {http://dx.doi.org/10.1016/j.colsurfb.2021.111696},
   keywords = {PEG; protein stabilizer; Crowding agent; excluded volume; protein unfolding},
   language = {eng},
   issn = {0927-7765},
   journal = {Colloids and Surfaces B: Biointerfaces},
   title = {Polyethylene glycol perturbs the unfolding of CRABP I: A correlation between experimental and theoretical approach},
   url = {https://doi.org/10.1016/j.colsurfb.2021.111696},
   volume = {202},
   year = {2021}
}

TY  - JOUR
ID  - 1753483
AU  - Subadini, Suchismita - Bera, Krishnendu - Hritz, Jozef - Sahoo, Harekrushna
PY  - 2021
TI  - Polyethylene glycol perturbs the unfolding of CRABP I: A correlation between experimental and theoretical approach
JF  - Colloids and Surfaces B: Biointerfaces
VL  - 202
IS  - June
SP  - 111696
EP  - 111696
PB  - Elsevier
SN  - 09277765
KW  - PEG
KW  - protein stabilizer
KW  - Crowding agent
KW  - excluded volume
KW  - protein unfolding
UR  - https://doi.org/10.1016/j.colsurfb.2021.111696
N2  - 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.
ER  -

SUBADINI, Suchismita, Krishnendu BERA, Jozef HRITZ a Harekrushna SAHOO. Polyethylene glycol perturbs the unfolding of CRABP I: A correlation between experimental and theoretical approach. \textit{Colloids and Surfaces B: Biointerfaces}. Elsevier, 2021, roč.~202, June, s.~111696-111705. ISSN~0927-7765. Dostupné z: https://dx.doi.org/10.1016/j.colsurfb.2021.111696.

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