Acetyl-11-keto-β-boswellic acid derivatives effects on the monomer and dimer structure of Aβ(1-40) and Aβ(1-42) peptides: molecular dynamics simulation approach

Peptides Aβ(1-40) and Aβ(1-42) are effective peptides in Alzheimer's disease. With the aggregation of these peptides outside the nerve cell, disease occurs. Drugs that reduce this accumulation prevent the progression of Alzheimer's. In this regard, herbal medicines are receiving more attention due to their less side effects. Due to its antioxidant properties, boswellia is effective in reducing the progression of neurological diseases. In this work, effects of Acetyl-11-keto-β-boswellic acid derivatives on the monomer and dimer structure of Aβ (1-40) and Aβ (1-42) peptides are monitored by using molecular dynamics simulation. The results showed that in the presence of ligand, the flexibility of the C-terminal residues of Aβ (1-40) is higher. The ligand also reduces the amount of peptide sheets. By calculating the conformation factor, the afinity of the ligand to interact with each of the peptide residues was calculated. The results of this calculation showed that the residues that tend to be binded have less flexibility. By calculating the free binding energy, the binding site of the ligands was determined.