Entrapment of A Beta 1-40 peptide in unstructured aggregates (Articolo in rivista)

Type
Label
  • Entrapment of A Beta 1-40 peptide in unstructured aggregates (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1088/0953-8984/24/24/244103 (literal)
Alternative label
  • Corsale C; Carrotta R; Mangione MR; Vilasi S; Provenzano A; Cavallaro G; Bulone D; San Biagio PL (2012)
    Entrapment of A Beta 1-40 peptide in unstructured aggregates
    in Journal of physics. Condensed matter (Print); IOP Publishing Ltd., Bristol BS1 6BE (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Corsale C; Carrotta R; Mangione MR; Vilasi S; Provenzano A; Cavallaro G; Bulone D; San Biagio PL (literal)
Pagina inizio
  • 244103 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://iopscience.iop.org/0953-8984/24/24/244103 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 24 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 24 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biofisica at Palermo, CNR, via Ugo La Malfa 153, I-90146, Palermo, Italy; Dipartimento di Scienze e Tecnologie Molecolari e Biomolecolari, Sezione di Chimica e Tecnologie Farmaceutiche, Università degli studi di Palermo, via Archirafi 32, I-90123 Palermo, Italy (literal)
Titolo
  • Entrapment of A Beta 1-40 peptide in unstructured aggregates (literal)
Abstract
  • Recognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that A?-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid ?-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggregates. They appear stable or at least metastable with respect to fiber growth, therefore appearing as an incidental product in the pathway of fibrillogenesis. (literal)
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