title: Natural biomolecules and protein aggregation: emerging strategies against amyloidogenesis.
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.
authors.affiliation: Institute of Biophysics, CNR, Italian National Research Council, Via G. Moruzzi 1, 56124 Pisa, Italy. antonella.sgarbossa@pi.ibf.cnr.it.
authors.forename: Antonella
authors.initials: A
authors.lastname: Sgarbossa
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D000686:Amyloidosis / Q000188:drug therapy / Q000378:metabolism / Q000473:pathology; D000818:Animals; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D019636:Neurodegenerative Diseases / Q000188:drug therapy / Q000378:metabolism / Q000473:pathology; D059808:Polyphenols / Q000627:therapeutic use*; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D059808:Polyphenols