New Human Islet Amyloid Polypeptide Fragments Susceptible to Aggregation

Author:

Rozniakowski Kamil1,Fraczyk Andrzej2,Galecki Krystian3,Wietrzyk Joanna4,Filip‐Psurska Beata4,Fraczyk Justyna1,Kaminski Zbigniew J.1ORCID,Kolesinska Beata1ORCID

Affiliation:

1. Institute of Organic Chemistry Faculty of Chemistry Lodz University of Technology Zeromskiego 116 Lodz 90-924 Poland

2. Institute of Applied Computer Science Lodz University of Technology Stefanowskiego Łódź, 18/22 Lodz 90-537 Poland

3. Institute of General Food Chemistry Faculty of Biotechnology and Food Sciences Lodz University of Technology Stefanowskiego 4/10 Lodz 90-924 Poland

4. Hirszfeld Institute of Immunology and Experimental Therapy Polish Academy of Sciences 12 Rudolfa Weigla St. 53-114 Wroclaw Poland

Publisher

Wiley

Subject

Molecular Biology,Molecular Medicine,General Chemistry,Biochemistry,General Medicine,Bioengineering

Reference61 articles.

1. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.

2. International Diabetes Federation. IDF Diabetes Atlas 8th edn. Brussels Belgium: International Diabetes Federation 2017. http://www.diabetesatlas.org; last accessed on January 23 2019.

3. W. F. Ganong ‘Review of Medical Physiology’ McGraw-Hill Appleton & Lange 21st edition 2003.

4. Amyloidogenicity and cytotoxicity of islet amyloid polypeptide

5. A mechanistic approach for islet amyloid polypeptide aggregation to develop anti-amyloidogenic agents for type-2 diabetes

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