Alpha-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Alpha-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (Articolo in rivista) (literal)

Anno

• 2013-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1038/srep02781 (literal)

Alternative label

• Pannuzzo M.; Raudino A.; Milardi D.; La Rosa C.; Karttunen M. (2013)
  Alpha-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes
  in Scientific reports (Nature Publishing Group)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Pannuzzo M.; Raudino A.; Milardi D.; La Rosa C.; Karttunen M. (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://www.scopus.com/inward/record.url?eid=2-s2.0-84885110787&partnerID=q2rCbXpz (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 3 (literal)

Rivista

• Scientific reports (Rivista)

Note

• Scopu (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Department of Computational Biology, University of Erlangen-Nuremberg, Staudtstr. 5, 91058 Erlangen, Germany; Department of Chemical Sciences, University of Catania, Viale Andrea Doria 6, Catania, Italy I-95125, Italy; Istituto di Biostrutture e Bioimmagini, CNR, Unita Organizzativa e di Supporto di Catania, Viale A. Doria 6, Catania, Italy I-95125, Italy; Department of Chemistry and Waterloo Institute for Nanotechnology, University of Waterloo, 200 University Avenue West, Waterloo, ON, N2L 3G1, Canada (literal)

Titolo

• Alpha-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (literal)

Abstract

• The human islet amyloid polypeptide (hIAPP) is the primary component in the toxic islet amyloid deposits in type-2 diabetes. hIAPP self-assembles to aggregates that permeabilize membranes and constitutes amyloid plaques. Uncovering the mechanisms of amyloid self-assembly is the key to understanding amyloid toxicity and treatment. Although structurally similar, hIAPP's rat counterpart, the rat islet amyloid polypeptide (rIAPP), is non-toxic. It has been a puzzle why these peptides behave so differently. We combined multiscale modelling and theory to explain the drastically different dynamics of hIAPP and rIAPP: The differences stem from electrostatic dipolar interactions. hIAPP forms pentameric aggregates with the hydrophobic residues facing the membrane core and stabilizing water-conducting pores. We give predictions for pore sizes, the number of hIAPP peptides, and aggregate morphology. We show the importance of curvature-induced stress at the early stages of hIAPP assembly and the ?-helical structures over ?-sheets. This agrees with recent fluorescence spectroscopy experiments. (literal)

Prodotto di

• Progettazione e sintesi di nuovi composti bioattivi e loro veicolazione sito specifica. (PM.P01.003.002) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• DANILO MILARDI (Persona)

Insieme di parole chiave

• Keywords of "Alpha-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• DANILO MILARDI (Persona)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Progettazione e sintesi di nuovi composti bioattivi e loro veicolazione sito specifica. (PM.P01.003.002) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Scientific reports (Rivista)

Insieme di parole chiave di

• Keywords of "Alpha-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes" (Insieme di parole chiave)