The effect of fulvic acid on pre- and postaggregation state of A beta 17a42: Molecular dynamics simulation studies

Alzheimer's disease (AD), a neurodegenerative disorder, is directly related to the aggregation of A beta peptides. These peptides can self-assemble from monomers to higher oligomeric or fibrillar structures in a highly ordered and efficient manner. This self-assembly process is accompanied by a...

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Bibliographic Details
Published in:Biochimica et biophysica acta. Proteins and proteomics 2013-01, Vol.1834 (1), p.24-33
Main Authors: Verma, Sharad, Singh, Amit, Mishra, Abha
Format: Article
Language:English
Online Access:Get full text
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Summary:Alzheimer's disease (AD), a neurodegenerative disorder, is directly related to the aggregation of A beta peptides. These peptides can self-assemble from monomers to higher oligomeric or fibrillar structures in a highly ordered and efficient manner. This self-assembly process is accompanied by a structural transition of the aggregated proteins from their normal fold into a predominantly beta -sheet secondary structure. 14 ns molecular dynamics simulation revealed that fulvic acid interrupted the dimer formation of A beta 17a42 peptide while in its absence A beta 17a42 dimer formation occurred at similar to 12 ns. Additionally, fulvic acid disrupted the preformed A beta 17a42 trimer in a very short time interval (12 ns). These results may provide an insight in the drug design against A beta 17a42 peptide aggregation using fulvic acid as lead molecule against A beta 17a42 mediated cytotoxicity and neurodegeneration.
ISSN:1570-9639