Simulation of Pentapeptide Drug Interaction with β-Sheet-Rich Monomers of Aβ Protein for Alzheimer Treatment

Khandan, Vahid; Firoozabadi, Bahar; Saeidi, Mohammad Saeid

doi:10.22041/ijbme.2014.13288

Document Type : Full Research Paper

Authors

¹ M.Sc Student, Mechanical Engineering Department, Sharif University oh Technology

² Professor, Mechanical Engineering Department, Sharif University oh Technology

10.22041/ijbme.2014.13288

Abstract

A hallmark of Alzheimer disease (the most common type of dementia in the elderly) is the aggregation and deposition of toxic species ranging from small soluble oligomers to insoluble fibril plaques of Amyloid-Beta protein originates from the cleavage of APP by Beta and Gama Secretase (Amyloid Hypothesis). An attractive therapeutic approach to treat AD is to identify small ligands capable of binding to A-Beta monomers and reverse its amyloidosis process. Here, a peptide drug having the sequence of GLMVG which has been derived from the C-terminal of A-Beta was used as breaker for a monomer of Beta sheet rich structure. The combination of Docking and Molecular Dynamics methods were used for simulation of drug-receptor interaction. This simulation implied that pentapeptide altered secondary structure of A-Beta monomer and declined its stability. This study proved that pentapeptide is capable to reverse Beta-sheet formation and can be considered as an AD drug in other preclinical studies.

Keywords

Main Subjects

Targeted Drug Delivery / Smart Drug Delivery / Drug Targeting

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Iranian Journal of Biomedical Engineering

Simulation of Pentapeptide Drug Interaction with β-Sheet-Rich Monomers of Aβ Protein for Alzheimer Treatment

References

References

Volume 8, Issue 3 - Serial Number 3
September 2014
Pages 229-239

Simulation of Pentapeptide Drug Interaction with β-Sheet-Rich Monomers of Aβ Protein for Alzheimer Treatment

References

References

Volume 8, Issue 3 - Serial Number 3September 2014Pages 229-239

Volume 8, Issue 3 - Serial Number 3
September 2014
Pages 229-239