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Biophysical Reviews

, Volume 10, Issue 2, pp 453–462 | Cite as

Membrane-mediated amyloid deposition of human islet amyloid polypeptide

  • Kenji Sasahara
Review
First Online:
Received:
Accepted:

Abstract

Amyloid deposition of human islet amyloid polypeptide (hIAPP) within the islet of Langerhans is closely associated with type II diabetes mellitus. Accumulating evidence indicates that the membrane-mediated aggregation and subsequent deposition of hIAPP are linked to the dysfunction and death of insulin-producing pancreatic β-cells, but the molecular process of hIAPP deposition is poorly understood. In this review, I focus on recent in vitro studies utilizing model membranes to observe the membrane-mediated aggregation/deposition of hIAPP. Membrane surfaces can serve as templates for both hIAPP adsorption and aggregation. Using high-sensitivity surface analyzing/imaging techniques that can characterize the processes of hIAPP aggregation and deposition at the membrane surface, these studies provide valuable insights into the mechanism of membrane damage caused by amyloid deposition of the peptide.

Keywords

Islet amyloid polypeptide Amyloid deposition Model membranes Membrane disruption Type II diabetes mellitus 
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Notes

Compliance with ethical standards

Conflict of interest

Kenji Sasahara declares that he has no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by the author.

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© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2017

Authors and Affiliations

  1. 1.Institute for Protein ResearchOsaka UniversitySuitaJapan

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