Document Detail


Fulvic Acid Inhibits Aggregation and Promotes Disassembly of Tau Fibrils Associated with Alzheimer's Disease.
MedLine Citation:
PMID:  21785188     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Alzheimer's disease is a neurodegenerative disorder involving extracellular plaques (amyloid-β) and intracellular tangles of tau protein. Recently, tangle formation has been identified as a major event involved in the neurodegenerative process, due to the conversion of either soluble peptides or oligomers into insoluble filaments. At present, the current therapeutic strategies are aimed at natural phytocomplexes and polyphenolics compounds able to either inhibit the formation of tau filaments or disaggregate them. However, only a few polyphenolic molecules have emerged to prevent tau aggregation, and natural drugs targeting tau have not been approved yet. Fulvic acid, a humic substance, has several nutraceutical properties with potential activity to protect cognitive impairment. In this work we provide evidence to show that the aggregation process of tau protein, forming paired helical filaments (PHFs) in vitro, is inhibited by fulvic acid affecting the length of fibrils and their morphology. In addition, we investigated whether fulvic acid is capable of disassembling preformed PHFs. We show that the fulvic acid is an active compound against preformed fibrils affecting the whole structure by diminishing length of PHFs and probably acting at the hydrophobic level, as we observed by atomic force techniques. Thus, fulvic acid is likely to provide new insights in the development of potential treatments for Alzheimer's disease using natural products.
Authors:
Alberto Cornejo; José M Jiménez; Leonardo Caballero; Francisco Melo; Ricardo B Maccioni
Related Documents :
11993768 - Quantifying the phenolic content of freshwaters using simple assays with different unde...
20593898 - Miscanthus x giganteus bark organosolv fractionation: fate of lipophilic components and...
1158328 - A model of closely assembled consecutive enzymes on membranes: formation of hydroxycinn...
16028988 - Identification of ellagic acid conjugates and other polyphenolics in muscadine grapes b...
1475378 - Oxidative metabolism of n-phenyllinoleamide by human nasal polyps.
12656698 - Determination of the reduction in gastric acidity necessary to prevent pathological oes...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-7-22
Journal Detail:
Title:  Journal of Alzheimer's disease : JAD     Volume:  -     ISSN:  1875-8908     ISO Abbreviation:  -     Publication Date:  2011 Jul 
Date Detail:
Created Date:  2011-7-25     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9814863     Medline TA:  J Alzheimers Dis     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
International Center for Biomedicine (ICC), University of Chile, Ñuñoa, Santiago, Chile.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Atomic and electronic structure of ultrathin fluoride barrier layers at the oxide/Si interface.
Next Document:  Lack of Association Between COMT Polymorphisms and Apathy in Alzheimer's Disease.