http://www.cnr.it/ontology/cnr/individuo/prodotto/ID208324
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)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Pagina inizio
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- 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
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
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- 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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