title: The effect of fulvic acid on pre- and postaggregation state of Aβ(17-42): molecular dynamics simulation studies.
abstract: Alzheimer's disease (AD), a neurodegenerative disorder, is directly related to the aggregation of Aβ 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 β-sheet secondary structure. 14ns molecular dynamics simulation revealed that fulvic acid interrupted the dimer formation of Aβ(17-42) peptide while in its absence Aβ(17-42) dimer formation occurred at ~12ns. Additionally, fulvic acid disrupted the preformed Aβ(17-42) trimer in a very short time interval (12ns). These results may provide an insight in the drug design against Aβ(17-42) peptide aggregation using fulvic acid as lead molecule against Aβ(17-42) mediated cytotoxicity and neurodegeneration.
authors.affiliation: School of Biochemical Engineering, Indian Institute of Technology (Banaras Hindu University), Varanasi-221005, India.
authors.forename: Sharad
authors.initials: S
authors.lastname: Verma
authors.forename: Amit
authors.initials: A
authors.lastname: Singh
authors.forename: Abha
authors.initials: A
authors.lastname: Mishra
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D001578:Benzopyrans / Q000737:chemistry*; D006801:Humans; D056004:Molecular Dynamics Simulation; D055503:Protein Multimerization; D017433:Protein Structure, Secondary
chemical_list: D016229:Amyloid beta-Peptides; D001578:Benzopyrans; C005023:fulvic acid