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Molecules 2015, 20(2), 2510-2528;

The Effect of Glycosaminoglycans (GAGs) on Amyloid Aggregation and Toxicity

Dipartimento di Biochimica, Biofisica e Patologia Generale, Seconda Università di Napoli, Via L. De Crecchio 7, Napoli 80138, Italy
Author to whom correspondence should be addressed.
Academic Editor: Vito Ferro
Received: 27 November 2014 / Accepted: 29 January 2015 / Published: 2 February 2015
(This article belongs to the Special Issue Glycosaminoglycans and Their Mimetics)
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Amyloidosis is a protein folding disorder in which normally soluble proteins are deposited extracellularly as insoluble fibrils, impairing tissue structure and function. Charged polyelectrolytes such as glycosaminoglycans (GAGs) are frequently found associated with the proteinaceous deposits in tissues of patients affected by amyloid diseases. Experimental evidence indicate that they can play an active role in favoring amyloid fibril formation and stabilization. Binding of GAGs to amyloid fibrils occurs mainly through electrostatic interactions involving the negative polyelectrolyte charges and positively charged side chains residues of aggregating protein. Similarly to catalyst for reactions, GAGs favor aggregation, nucleation and amyloid fibril formation functioning as a structural templates for the self-assembly of highly cytotoxic oligomeric precursors, rich in β-sheets, into harmless amyloid fibrils. Moreover, the GAGs amyloid promoting activity can be facilitated through specific interactions via consensus binding sites between amyloid polypeptide and GAGs molecules. We review the effect of GAGs on amyloid deposition as well as proteins not strictly related to diseases. In addition, we consider the potential of the GAGs therapy in amyloidosis. View Full-Text
Keywords: glycosaminoglycans; amyloid aggregation; amyloid toxicity inhibition glycosaminoglycans; amyloid aggregation; amyloid toxicity inhibition

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Iannuzzi, C.; Irace, G.; Sirangelo, I. The Effect of Glycosaminoglycans (GAGs) on Amyloid Aggregation and Toxicity. Molecules 2015, 20, 2510-2528.

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