Integrating in vitro and in silico approaches to evaluate the “dual functionality” of palmatine chloride in inhibiting and disassembling Tau-derived VQIVYK peptide fibrils

• Published in: Biochimica et biophysica acta Vol. 1862; no. 7; pp. 1565 - 1575
• Main Authors: Haj, Esraa, Losev, Yelena, Guru KrishnaKumar, V., Pichinuk, Edward, Engel, Hamutal, Raveh, Avi, Gazit, Ehud, Segal, Daniel
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.07.2018
• Subjects: Adrenal Gland Neoplasms - pathology; Aggregation modulator; Amyloid; Amyloid - drug effects; Amyloid - ultrastructure; Berberine Alkaloids - pharmacology; Circular Dichroism; Computer Simulation; High-Throughput Screening; High-Throughput Screening Assays; Humans; In Vitro Techniques; Molecular Docking Simulation; Palmatine; Peptide Fragments - chemistry; Peptide Fragments - drug effects; Pheochromocytoma - pathology; PHF6 peptide; Protein Aggregation, Pathological; Tau protein; tau Proteins - chemistry; tau Proteins - drug effects; Tumor Cells, Cultured; Palmatine; High-Throughput Screening; Amyloid; PHF6 peptide; Aggregation modulator; Tau protein

Alzheimer's disease (AD) is the most common neurodegenerative disorder which is characterized by the deposits of intra-cellular tau protein and extra-cellular amyloid-β (Aβ) peptides in the human brain. Understanding the mechanism of protein aggregation and finding compounds that are capable of...