Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis (Articolo in rivista)

Type
Label
  • Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.3390/ijms131217121 (literal)
Alternative label
  • Sgarbossa A (2012)
    Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis
    in International journal of molecular sciences (Online); MDPI AG, Basel (Swaziland)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Sgarbossa A (literal)
Pagina inizio
  • 17121 (literal)
Pagina fine
  • 17137 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.mdpi.com/1422-0067/13/12/17121 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 13 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 12 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Italian Natl Res Council, CNR, Inst Biophys, I-56124 Pisa, Italy (literal)
Titolo
  • Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis (literal)
Abstract
  • Biomolecular self-assembly is a fundamental process in all organisms. As primary components of the life molecular machinery, proteins have a vast array of resources available to them for self-assembly in a functional structure. Protein self-assembly, however, can also occur in an aberrant way, giving rise to non-native aggregated structures responsible for severe, progressive human diseases that have a serious social impact. Different neurodegenerative disorders, like Huntington's, Alzheimer's, and spongiform encephalopathy diseases, have in common the presence of insoluble protein aggregates, generally termed \"amyloid,\" that share several physicochemical features: a fibrillar morphology, a predominantly beta-sheet secondary structure, birefringence upon staining with the dye Congo red, insolubility in common solvents and detergents, and protease resistance. Conformational constrains, hydrophobic and stacking interactions can play a key role in the fibrillogenesis process and protein-protein and peptide-peptide interactions--resulting in self-assembly phenomena of peptides yielding fibrils--that can be modulated and influenced by natural biomolecules. Small organic molecules, which possess both hydrophilic and hydrophobic moieties able to bind to peptide/protein molecules through hydrogen bonds and hydrophobic and aromatic interactions, are potential candidates against amyloidogenesis. In this review some significant case examples will be critically discussed. (literal)
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