Calorimetry and FTIR reveal the ability of URG7 protein to modify the aggregation state of both cell lysate and amylogenic α-synuclein

Jany Dandurand; Angela Ostuni; Maria Francesca Armentano; Maria Antonietta Crudele; Vincenza Dolce; Federica Marra; Valérie Samouillan; Faustino Bisaccia; Jany Dandurand; Angela Ostuni; Maria Francesca Armentano; Maria Antonietta Crudele; Vincenza Dolce; Federica Marra; Valérie Samouillan; Faustino Bisaccia

doi:10.3934/biophy.2020015

AIMS Biophysics

2020, Volume 7, Issue 3: 189-203. doi: 10.3934/biophy.2020015

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Calorimetry and FTIR reveal the ability of URG7 protein to modify the aggregation state of both cell lysate and amylogenic α-synuclein

1.
CIRIMAT, Physique des Polymères, Université Paul Sabatier, Toulouse, France
2.
Department of Sciences, University of Basilicata, Potenza, Italy
3.
Department of Pharmacy, Health and Nutritional Sciences, University of Calabria, Italy

Received: 02 May 2020 Accepted: 15 June 2020 Published: 18 June 2020

Differential scanning calorimetry and FITR analyses allowed to investigate the role of URG7 (up-regulated gene clone 7) protein involved in the development of hepatocellular carcinoma induced by hepatitis B virus infection, on the physical structure both of lysates of human hepatoblastoma cells (HepG2) stressed with tunicamycin and α-synuclein, one of the proteins associated with neurogenerative diseases. The protein-water interfacial region was identified and correlated with protein structure. DSC results confirm through the interfacial water behavior that URG7 is able to act in two ways: it maintains the interfacial water stability and controls the mobile fraction level, thereby the flexibility and the protein folding. The mobile water phase increases strongly for cells exposed to α-synuclein, demonstrating an important influence on water hydration. FTIR results evidenced an increase of about 30% of cross β structures in cells exposed to α-synuclein, associated with aggregated proteins. In stress conditions, URG7 was able to maintain the same fraction of mobile water as untreated cells. URG7 was able to restore the water reorientation ability around the complex lysate system and reduced abnormal protein folding.
- URG7,
- Differential Scanning Calorimetry,
- physical structure,
- interfacial water,
- protein aggregation,
- synuclein
Citation: Jany Dandurand, Angela Ostuni, Maria Francesca Armentano, Maria Antonietta Crudele, Vincenza Dolce, Federica Marra, Valérie Samouillan, Faustino Bisaccia. Calorimetry and FTIR reveal the ability of URG7 protein to modify the aggregation state of both cell lysate and amylogenic α-synuclein[J]. AIMS Biophysics, 2020, 7(3): 189-203. doi: 10.3934/biophy.2020015

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Abstract

Differential scanning calorimetry and FITR analyses allowed to investigate the role of URG7 (up-regulated gene clone 7) protein involved in the development of hepatocellular carcinoma induced by hepatitis B virus infection, on the physical structure both of lysates of human hepatoblastoma cells (HepG2) stressed with tunicamycin and α-synuclein, one of the proteins associated with neurogenerative diseases. The protein-water interfacial region was identified and correlated with protein structure. DSC results confirm through the interfacial water behavior that URG7 is able to act in two ways: it maintains the interfacial water stability and controls the mobile fraction level, thereby the flexibility and the protein folding. The mobile water phase increases strongly for cells exposed to α-synuclein, demonstrating an important influence on water hydration. FTIR results evidenced an increase of about 30% of cross β structures in cells exposed to α-synuclein, associated with aggregated proteins. In stress conditions, URG7 was able to maintain the same fraction of mobile water as untreated cells. URG7 was able to restore the water reorientation ability around the complex lysate system and reduced abnormal protein folding.

Conflict of interest

The author declares no conflict of interest.

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