Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis
AbstractBiomolecular 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.
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Sgarbossa, A. Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis. Int. J. Mol. Sci. 2012, 13, 17121-17137.
Sgarbossa A. Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis. International Journal of Molecular Sciences. 2012; 13(12):17121-17137.Chicago/Turabian Style
Sgarbossa, Antonella. 2012. "Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis." Int. J. Mol. Sci. 13, no. 12: 17121-17137.