Gallic acid loaded onto polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA-GA NPs) stabilizes α-synuclein in the unfolded conformation and inhibits aggregation-Reference-Cited by-同舟云学术

Gallic acid loaded onto polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA-GA NPs) stabilizes α-synuclein in the unfolded conformation and inhibits aggregation

Published:2016 Issue:88 Volume:6 Page:85312-85323
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Mohammad-Beigi Hossein¹²³⁴⁵,Morshedi Dina⁶⁷⁸⁹,Shojaosadati Seyed Abbas⁵¹⁰¹¹⁸⁹,Pedersen Jannik Nedergaard¹²³⁴,Marvian Amir Tayaranian¹²²¹³⁴,Aliakbari Farhang⁶⁷⁸⁹¹⁴,Christiansen Gunna¹²²¹³⁴,Pedersen Jan Skov¹²³⁴¹⁵,Otzen Daniel E.¹²³⁴¹⁶

Affiliation:

1. Interdisciplinary Nanoscience Centre (iNANO)

2. Aarhus University

3. DK – 8000 Aarhus C

4. Denmark

5. Biotechnology Group

6. Department of Industrial and Environmental Biotechnology

7. National Institute of Genetic Engineering and Biotechnology

8. Tehran

9. Iran

10. Faculty of Chemical Engineering

11. Tarbiat Modares University

12. Department of Biomedicine-Medical Microbiology and Immunology

13. 8000 Aarhus C

14. Student Research Committee and Department of Medical Biotechnology

15. Department of Chemistry

16. Department of Molecular Biology and Genetics

Abstract

The aggregation of the 140-residue protein α-synuclein (αSN) plays a major role in the pathogenesis of different neurodegenerative disorders such as Parkinson's Disease (PD).

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/RA/C6RA08502D

Reference48 articles.

1. Genes and parkinsonism

2. Identification of two distinct synucleins from human brain

3. α-Synuclein in Lewy bodies

4. Amyloid pores from pathogenic mutations

5. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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