Journal of Diabetes Research

Recent Insight in Islet Amyloid Polypeptide Morphology, Structure, Membrane Interaction, and Toxicity in Type 2 Diabetes


Status
Published

1UPMC, Paris, France

2Tel Aviv University, Tel Aviv, Israel

3Yale University, New Haven, USA


Recent Insight in Islet Amyloid Polypeptide Morphology, Structure, Membrane Interaction, and Toxicity in Type 2 Diabetes

Description

The formation of protein amyloid deposits is associated with major human diseases including Alzheimer's disease, Parkinson's disease, the spongiform encephalopathy, and type 2 diabetes mellitus. Type 2 diabetes mellitus is characterized metabolically by defects in both insulin secretion and insulin action, resulting in hyperglycemia, and is characterized histopathologically by the presence of fibrillar amyloid deposits in the pancreatic islets of Langerhans (islet amyloid). The presence of these amyloid deposits has been linked to death of the insulin-producing islet β-cells.

Islet amyloid polypeptide (IAPP), a 37-amino-acid peptide, is the major constituent of the amyloid deposits found in type 2 diabetic patients. Despite considerable progress, there are important outstanding issues in the field of islet amyloid.

Advances in biophysical methods will aid our understanding of the process of IAPP amyloid formation. We invite authors to submit original research and review articles that seek to define the molecular and cellular mechanism of amyloid formation. We are interested in articles that explore new aspects of peptide structure and dynamics, peptide-membrane interactions, new methodology to provide insight into the misfolding pathways, and so forth.

Potential topics include, but are not limited to:

  • Elucidation of the molecular mechanisms of IAPP
  • Identification of the toxic IAPP species
  • Potential drug development, small-molecule inhibitors
  • New structural information and kinetic studies on IAPP
  • Method development to characterize the structure and oligomerization of amyloid proteins

Articles

  • Special Issue
  • - Volume 2016
  • - Article ID 2535878
  • - Editorial

Recent Insight in Islet Amyloid Polypeptide Morphology, Structure, Membrane Interaction, and Toxicity in Type 2 Diabetes

Lucie Khemtemourian | Ehud Gazit | Andrew Miranker
  • Special Issue
  • - Volume 2016
  • - Article ID 7293063
  • - Review Article

New Insights from Sum Frequency Generation Vibrational Spectroscopy into the Interactions of Islet Amyloid Polypeptides with Lipid Membranes

Li Fu | Zhuguang Wang | ... | Elsa C. Y. Yan
  • Special Issue
  • - Volume 2016
  • - Article ID 1749196
  • - Research Article

Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid Bilayers

Zhenyu Qian | Yan Jia | Guanghong Wei
  • Special Issue
  • - Volume 2016
  • - Article ID 2798269
  • - Review Article

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology

Rehana Akter | Ping Cao | ... | Daniel P. Raleigh
  • Special Issue
  • - Volume 2016
  • - Article ID 2046327
  • - Review Article

Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives

Amit Pithadia | Jeffrey R. Brender | ... | Ayyalusamy Ramamoorthy
  • Special Issue
  • - Volume 2016
  • - Article ID 5639875
  • - Review Article

Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus

Lucie Caillon | Anais R. F. Hoffmann | ... | Lucie Khemtemourian
  • Special Issue
  • - Volume 2015
  • - Article ID 918573
  • - Review Article

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

Marianna Flora Tomasello | Alessandro Sinopoli | Giuseppe Pappalardo
  • Special Issue
  • - Volume 2015
  • - Article ID 849017
  • - Review Article

The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP

Mimi Gao | Roland Winter
  • Special Issue
  • - Volume 2015
  • - Article ID 946037
  • - Research Article

Charge-Based Inhibitors of Amylin Fibrillization and Toxicity

Sharadrao M. Patil | Andrei T. Alexandrescu
  • Special Issue
  • - Volume 2015
  • - Article ID 515307
  • - Review Article

Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis

Phuong Trang Nguyen | Nagore Andraka | ... | Steve Bourgault
Journal of Diabetes Research
 Journal metrics
Acceptance rate32%
Submission to final decision68 days
Acceptance to publication26 days
CiteScore5.500
Impact Factor2.965
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