Vitamin k3 inhibits protein aggregation: Implication in the treatment of amyloid diseases

• DOI: 10.1038/srep26759
• Publication Date: 2016-05-27T09:59:46Z
• Authors: Parvez Alam; Sumit Kumar Chatu...; Mohammad Khurshee...; Ravi Kant Rajpoot; Mohd Rehan Ajmal; Masihuz Zaman; Rizwan Hasan Khan
• Keywords: Fibrillogenesis; Thioflavin; Amyloid (mycology); Amyloid disease; Melittin

Abstract Protein misfolding and aggregation have been associated with several human diseases such as Alzheimer’s, Parkinson’s familial amyloid polyneuropathy etc. In this study, anti-fibrillation activity of vitamin k3 its effect on the kinetics formation hen egg white lysozyme (HEWL) Aβ-42 peptide were investigated. Here, in combination Thioflavin T (ThT) fluorescence assay, circular dichroism (CD), transmission electron microscopy cell cytotoxicity we demonstrated that significantly inhibits fibril well inhibitory is dose dependent manner. Our experimental studies inferred exert neuro protective against induced through concerted pathway, modifying towards nontoxic aggregates. Molecular docking mediated inhibition HEWL fibrillogenesis may be initiated by interacting proteolytic resistant prone regions respectively. This work would provide an insight into mechanism protein k3; pave way for discovery other small molecules similar neurodegenerative diseases.