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Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis

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, givin...

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Autor principal: Sgarbossa, Antonella
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3546742/
https://www.ncbi.nlm.nih.gov/pubmed/23242152
http://dx.doi.org/10.3390/ijms131217121
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author Sgarbossa, Antonella
author_facet Sgarbossa, Antonella
author_sort Sgarbossa, Antonella
collection PubMed
description 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.
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spelling pubmed-35467422013-01-23 Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis Sgarbossa, Antonella Int J Mol Sci Review 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. Molecular Diversity Preservation International (MDPI) 2012-12-14 /pmc/articles/PMC3546742/ /pubmed/23242152 http://dx.doi.org/10.3390/ijms131217121 Text en © 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Sgarbossa, Antonella
Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis
title Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis
title_full Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis
title_fullStr Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis
title_full_unstemmed Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis
title_short Natural Biomolecules and Protein Aggregation: Emerging Strategies against Amyloidogenesis
title_sort natural biomolecules and protein aggregation: emerging strategies against amyloidogenesis
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3546742/
https://www.ncbi.nlm.nih.gov/pubmed/23242152
http://dx.doi.org/10.3390/ijms131217121
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