Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization

Aseem Mishra, Anurag Misra, T. Sri Vaishnavi, Chaitanya Thota, Madhvi Gupta, Suryanarayanarao Ramakumar, Virander Singh Chauhan

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

hIAPP fibrillization implicated in Type 2 diabetes pathology involves formation of oligomers toxic to insulin producing pancreatic β-cells. We report design, synthesis, 3D structure and functional characterization of dehydrophenylalanine (ΔF) containing peptides which inhibit hIAPP fibrillization. The inhibitor protects β-cells from hIAPP induced toxicity.

Original languageEnglish (US)
Pages (from-to)2688-2690
Number of pages3
JournalChemical Communications
Volume49
Issue number26
DOIs
StatePublished - Mar 5 2013

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ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry(all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

Cite this

Mishra, A., Misra, A., Sri Vaishnavi, T., Thota, C., Gupta, M., Ramakumar, S., & Chauhan, V. S. (2013). Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization. Chemical Communications, 49(26), 2688-2690. https://doi.org/10.1039/c3cc38982k