Molecular and cytotoxic properties of hIAPP17-29 and rIAPP17-29 fragments: A comparative study with the respective full-length parent polypeptides (Articolo in rivista)

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  • Molecular and cytotoxic properties of hIAPP17-29 and rIAPP17-29 fragments: A comparative study with the respective full-length parent polypeptides (Articolo in rivista) (literal)
Anno
  • 2014-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.ejmech.2014.05.038 (literal)
Alternative label
  • Tomasello, Marianna Flora; Sinopoli, Alessandro; Attanasio, Francesco; Giuffrida, Maria Laura; Campagna, Tiziana; Milardi, Danilo; Pappalardo, Giuseppe (2014)
    Molecular and cytotoxic properties of hIAPP17-29 and rIAPP17-29 fragments: A comparative study with the respective full-length parent polypeptides
    in European journal of medicinal chemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Tomasello, Marianna Flora; Sinopoli, Alessandro; Attanasio, Francesco; Giuffrida, Maria Laura; Campagna, Tiziana; Milardi, Danilo; Pappalardo, Giuseppe (literal)
Pagina inizio
  • 442 (literal)
Pagina fine
  • 455 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 81 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 14 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR-Institute of Biostructures and Bioimaging, Via P. Gaifami 18, 95126 Catania, Italy International PhD Program in Translational Biomedicine, University of Catania, V.le A. Doria 6, 95125 Catania, Italy (literal)
Titolo
  • Molecular and cytotoxic properties of hIAPP17-29 and rIAPP17-29 fragments: A comparative study with the respective full-length parent polypeptides (literal)
Abstract
  • The human islet polypeptide (hIAPP) or amylin is a 37-residue peptide hormone secreted by beta-cells of the islet of Langerhans in the pancreas. Unlike the rat variant of IAPP (rIAPP), human amylin is highly amyloidogenic and is found as amyloid deposits in nearly 95% of patients afflicted with type 2 diabetes mellitus (T2DM). Human and rat IAPP have nearly identical primary sequence differing at only six positions which are encompassed within the 17-29 aminoacid region. Using Circular Dichroism (CD), Dynamic Light Scattering (DLS) and ThT-fluorescence (Th-T), we examined the aggregation properties of both full-length hIAPP1-37 and the related peptide fragment hIAPP17-29. For the sake of comparison, similar experiments were carried out on the respective rat variants rIAPP1-37 and rIAPP17-29. These studies were conducted at physiological pH in buffered solution not containing fluorinated co-solvents as well as in the presence of model membranes (LUV). In addition, the cytotoxic activity of the investigated peptides was determined toward different pancreatic beta-cell lines. All the peptide studied in this work resulted cytotoxic despite beta-sheet structure being observed, in vitro, for the hIAPP1-37 only. This suggests that beta-sheet conformational transition that generally precedes the fibril formation, is not a prerequisite for toxicity towards beta-cells. Interestingly, confocal microscopy indicated that the IAPP peptides can enter the cell and might exert their toxic action at an intracellular level. (C) 2014 Elsevier Masson SAS. All rights reserved. (literal)
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