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Molecular docking studies on the interaction of anti-alzheimer compounds with amyloid beta peptides


Faujan, Nur Hana and Zakaria, Norzalina and Mohammad, Nurul Najihah (2019) Molecular docking studies on the interaction of anti-alzheimer compounds with amyloid beta peptides. Journal of Multidisciplinary Engineering Science and Technology (JMEST), 6 (12). pp. 132-136. ISSN 2458-9403


Alzheimer’s disease is a neurodegenerative disorder. Aggregation of amyloid β-peptide (Aβ42) into fibrils is a key pathological process associated with Alzheimer’s disease. In this study, effect of surfactin against amyloid β-peptide was studied by using computational approaches. In the molecular docking, surfactin interacts with A chain of amyloid fibril and forms the hydrogen bonds with Ala 21 and Asp 23 with total energy of −3.28 kcal/mol. Surfactin interacts with an amphiphilic pore amyloid β-peptide (Aβ42); binding of surfactin to amyloid fiber shows the decrease in salt bridge length (between Asp 23 and Lys 28) from 11.5 to 9.0 Å; and this may lead to displace the water molecules and so destabilize the amyloid β-peptide (Aβ42). 10-ns molecular dynamics simulation was performed for amyloid fibril and with surfactin amyloid fibril complex. RMSD, RMSF, Rg trajectories, and SASA plot further used to study the stability of complex and effect of surfactin. This is the novel in silico study of surfactin against the amyloid β-peptide (Aβ42) fiber responsible for Alzheimer’s disease, and these results may provide an insight role of surfactin in the drug design against Alzheimer’s disease.

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Additional Metadata

Item Type: Article
Divisions: Faculty of Science
Centre of Foundation Studies for Agricultural Science
Publisher: Bitlis
Keywords: Molecular docking; Amyloid beta peptide; Hydrogen bonding; Alzheimer’s
Depositing User: Ms. Nida Hidayati Ghazali
Date Deposited: 13 Feb 2021 19:48
Last Modified: 13 Feb 2021 19:48
URI: http://psasir.upm.edu.my/id/eprint/81410
Statistic Details: View Download Statistic

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