Tanshinones inhibit hIAPP aggregation, disaggregate preformed hIAPP fibrils, and protect cultured cells-Reference-Cited by-同舟云学术

Tanshinones inhibit hIAPP aggregation, disaggregate preformed hIAPP fibrils, and protect cultured cells

Published:2018 Issue:1 Volume:6 Page:56-67
ISSN:2050-750X
Container-title:Journal of Materials Chemistry B
language:en
Short-container-title:J. Mater. Chem. B

Author:

Ren Baiping¹²³⁴⁵,Liu Yonglan⁶⁷⁸⁹,Zhang Yanxian⁶⁷⁸⁹,Zhang Mingzhen⁶⁷⁸⁹,Sun Yan¹⁰¹¹¹²¹³¹⁴,Liang Guizhao¹⁵¹⁶¹⁷¹⁸¹⁴,Xu Jianxiong¹²³⁴⁵,Zheng Jie⁶⁷⁸⁹^ORCID

Affiliation:

1. Hunan Key Laboratory of Biomedical Nanomaterials and Devices

2. College of Life Science and Chemistry

3. Hunan University of Technology

4. Zhuzhou 412007

5. P. R. China

6. Department of Chemical & Biomolecular Engineering

7. The University of Akron

8. Ohio 44325

9. USA

10. Department of Biochemical Engineering

11. Key Laboratory of Systems Bioengineering of the Ministry of Education School of Chemical Engineering and Technology

12. Tianjin University

13. Tianjin 300072

14. China

15. Key Laboratory of Biorheological Science and Technology

16. Ministry of Education College

17. Chongqing University

18. Chongqing 400044

Abstract

Tanshinones act as common inhibitors to inhibit the aggregation of both hIAPP and Aβ, disaggregate preformed hIAPP and Aβ amyloid fibrils, and protect cells from hIAPP- and Aβ-induced toxicity.

Funder

Division of Chemical, Bioengineering, Environmental, and Transport Systems

Alzheimer's Association

National Natural Science Foundation of China

Division of Materials Research

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science,Biomedical Engineering,General Chemistry,General Medicine

Link

http://pubs.rsc.org/en/content/articlepdf/2018/TB/C7TB02538F

Reference55 articles.

1. On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides

2. Islet Amyloid in Type 2 Diabetes, and the Toxic Oligomer Hypothesis

3. Seed-Induced Heterogeneous Cross-Seeding Self-Assembly of Human and Rat Islet Polypeptides

4. Interfacial interaction and lateral association of cross-seeding assemblies between hIAPP and rIAPP oligomers

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