title: Mutation-based structural modification and dynamics study of amyloid beta peptide (1-42): An in-silico-based analysis to cognize the mechanism of aggregation.
abstract: Alzheimer's disease is the prevalent cause of premature senility, a progressive mental disorder due to degeneration in brain and deposition of amyloid β peptide (1-42, a misfolded protein) in the form of aggregation that prevails for a prolonged time and obstructs every aspect of life. One of the primary hallmarks of the neuropathological disease is the accretion of amyloid β peptide in the brain that leads to Alzheimer's disease, but the mechanism is still a mystery. Several investigations have shown that mutations at specific positions have a significant impact in stability of the peptide as predicted from aggregation profiles. Here in our study, we have analyzed the mutations by substituting residues at position A22G, E22G, E22K, E22Q, D23N, L34V and molecular dynamics have been performed to check the deviation in stability and conformation of the peptide. The results validated that the mutations at specific positions lead to instability and the proline substitution at E22P and L34P stalled the aggregation of the peptide.
authors.affiliation: School of Biotechnology and Bioinformatics, D.Y. Patil University, Navi Mumbai, India.
authors.forename: Pritam Kumar
authors.initials: PK
authors.lastname: Panda
authors.affiliation: School of Biotechnology and Bioinformatics, D.Y. Patil University, Navi Mumbai, India.
authors.forename: Abhaysinha Satish
authors.initials: AS
authors.lastname: Patil
authors.affiliation: School of Biotechnology and Bioinformatics, D.Y. Patil University, Navi Mumbai, India.
authors.forename: Priyam
authors.initials: P
authors.lastname: Patel
authors.affiliation: Gujarat Agricultural Biotechnology Institute, Navsari Agricultural University, Athwa Farm, Ghod Dod Road, Surat, Gujarat, India.
authors.forename: Hetalkumar
authors.initials: H
authors.lastname: Panchal
keywords: Aggregation; Alzheimer's disease; Amyloid β peptide; Discovery Studio Visualizer; Mutational analysis; NAMD; UCSF Chimera