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Design and study of peptide-based inhibitors of amylin cytotoxicity
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
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2010 (English)In: Bioorganic & Medicinal Chemistry Letters, ISSN 0960-894X, E-ISSN 1464-3405, Vol. 20, no 4, 1360-1362 p.Article in journal (Refereed) Published
Abstract [en]

The incidence of type II diabetes is on the increase each year and the World Health Organisation (WHO) predicts there to be over 360 million diabetic patients worldwide by the year 2030. Deposits consisting mainly of a small protein, called islet amyloid polypeptide (amylin), which aggregates into oligo-/polymeric beta sheet structures is responsible for cytoxicity to the pancreatic beta-cells, thus inhibition of this process has been explored as a potential prevention or treatment. N-Methylated and non N-methylated peptides spanning the length of amylin(1-37) were synthesised and evaluated for their inhibition of full length amylin mediated cytoxicity to RIN-5F cells. The non N-methylated peptides were very effective in inhibiting the cytotoxicity while the N-methylated peptides were not. Both the N-methylated and non N-methylated versions of the 29-34 region were equally effective.

Place, publisher, year, edition, pages
2010. Vol. 20, no 4, 1360-1362 p.
Keyword [en]
N-Methylated, Peptides, Amylin, Cytotoxicity
National Category
Pharmaceutical Sciences
URN: urn:nbn:se:uu:diva-138049DOI: 10.1016/j.bmcl.2010.01.004ISI: 000274285600009PubMedID: 20093026OAI: oai:DiVA.org:uu-138049DiVA: diva2:378819
Available from: 2010-12-16 Created: 2010-12-16 Last updated: 2010-12-16Bibliographically approved

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