Aggregation properties of the peptide fragments derived from the 17-29 region of the human and rat IAPP: a comparative study with two new PEG-conjugated variants of the human sequence. (Articolo in rivista)

Type
Label
  • Aggregation properties of the peptide fragments derived from the 17-29 region of the human and rat IAPP: a comparative study with two new PEG-conjugated variants of the human sequence. (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jp908436s (literal)
Alternative label
  • A. Mazzaglia; N. Micali; L.Scolaro; F. Attanasio; A. Magrì; G. Pappalardo; V. Villari (2010)
    Aggregation properties of the peptide fragments derived from the 17-29 region of the human and rat IAPP: a comparative study with two new PEG-conjugated variants of the human sequence.
    in The journal of physical chemistry. B
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • A. Mazzaglia; N. Micali; L.Scolaro; F. Attanasio; A. Magrì; G. Pappalardo; V. Villari (literal)
Pagina inizio
  • 705 (literal)
Pagina fine
  • 713 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 114 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • N. Micali; L.Scolaro Univ Messina, Dipartimento Chim Inorgan Chim Analit & Chim Fis, CNR, Ist Studio Mat Nanostrutturati, I-98166 Messina, Italy (literal)
Titolo
  • Aggregation properties of the peptide fragments derived from the 17-29 region of the human and rat IAPP: a comparative study with two new PEG-conjugated variants of the human sequence. (literal)
Abstract
  • The amyloidogenic amino acid sequence Ac-VHSSNNFGAILSS-NH(2), corresponding to the 17-29 peptide region of human amylin (hIAPP17-29), was modified by grafting a hydrophilic PEG chain in order to obtain a novel class of peptides to be used as models to study the aggregation process of the full-length IAPP. The amphiphilic feature of the pegylated peptide fragment at the N-terminus (PEG-N-hIAPP17-29) drives the aggregation process toward stable micellar clusters without fibrillogenesis, despite the presence of P-sheet interaction between peptides at pH values higher than 4.0. The hIAPP17-29-C-PEG, in which the PEG moiety is linked to the C-terminus, does not possess analogous amphiphilic character and the ability of PEG in forming H-bonds with the solvent overcomes that of the peptide chain, thereby causing peptide flocculation. The comparison with the unmodified hIAPP17-29 and the rat's peptide sequence Ac-VRSSNNLGPGLPP-NH(2)(rIAPP17-29) revealed the crucial role of hydrogen bonding between peptide and solvent in determining the aggregate structure and preventing fibril formation, as well as the non-negligible effect of a small amount of organic solvent in the aqueous Solution which affects the aggregation process and rate. (literal)
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