Int. J. Mol. Sci. 2012, 13(12), 17121-17137; doi:10.3390/ijms131217121
Review

Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis

Received: 29 November 2012; in revised form: 12 December 2012 / Accepted: 12 December 2012 / Published: 14 December 2012
(This article belongs to the Special Issue Molecular Self-Assembly 2012)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
Keywords: proteins; peptides; self-assembly; misfolding; aggregation; amyloid; fibrillogenesis; natural molecules; polyphenols; aromatic molecules
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MDPI and ACS Style

Sgarbossa, A. Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis. Int. J. Mol. Sci. 2012, 13, 17121-17137.

AMA Style

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.

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