Interfacial interaction and lateral association of cross-seeding assemblies between hIAPP and rIAPP oligomers-Reference-Cited by-同舟云学术

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

Published:2015 Issue:16 Volume:17 Page:10373-10382
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Zhang Mingzhen¹²³⁴,Hu Rundong¹²³⁴,Chen Hong¹²³⁴,Chang Yung⁵⁶⁷⁸,Gong Xiong⁹²³⁴,Liu Fufeng¹⁰¹¹¹²¹³¹⁴,Zheng Jie¹²³⁴

Affiliation:

1. Department of Chemical and Biomolecular Engineering

2. The University of Akron

3. Akron

4. USA

5. R&D Center for Membrane Technology and Department of Chemical Engineering

6. Chung Yuan University

7. Taoyuan 320

8. Taiwan

9. College of Polymer Science and Polymer Engineering

10. Department of Biochemical Engineering and Key Laboratory of Systems Bioengineering (Ministry of Education)

11. School of Chemical Engineering and Technology

12. Tianjin University

13. Tianjin 300072

14. China

Abstract

Cross-sequence interactions between different amyloid peptides are important not only for fundamental understanding of amyloid aggregation and polymorphism mechanisms, but also for probing a potential molecular link between different amyloid diseases.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2015/CP/C4CP05658B

Reference61 articles.

1. Natural oligomers of the amyloid-β protein specifically disrupt cognitive function

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

4. Islet Amyloid and Type 2 Diabetes Mellitus

5. Membrane Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective

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