The effect of PC20:0 and di-C7-PC amphiphilic surfactants on the aggregation of Aβ1-40 and Aβ1-42 using molecular dynamics simulation

At least 25 types of degenerative diseases are thought to be caused by amyloid-beta, including Alzheimer's. However, the exact mechanism of Alzheimer's is still unknown. It has been shown that amphiphilic surfactants with varying tail lengths, PC20:0 and di-C7-PC, have differing effects on the structures of A beta (1-40) and A beta (1-42). This paper examines the interaction between these surfactants and peptides. The calculations were performed at concentrations lower than the critical micelle concentration. Four and 12 peptides of beta-amyloid isomers regimens were used for each simulation. Direct and indirect behavioral effects were extensively investigated. A number of critical analyses, including RMSD, increment RMSF, P-i, and the hydration network, were performed to examine these peptides in the absence and presence of ligands. There can be a negative increment RMSF for each sequence as a result of ligand or surfactant binding to that sequence; otherwise, the structure is partially or locally folded. Demonstrated that PC20:0 and di-C7-PC amphiphilic surfactants affect the aggregation of A beta(1-40) and A beta(1-42). The results of our simulations showed that the negative values of Delta RMSF match with some P-i > 1 values for both the hydrophobic and hydrophilic sides of ligands. Therefore, potential interactions between residual peptides and ligands were identified. A negative Delta RMSF did not match the P-i > 1 value, indicating the folding behavior of peptide residues.

Automated summary

This paper examines the interaction between amyloid-beta and two different surfactants, showing their effects on the aggregation of the protein. The calculations suggest potential interactions between peptide residues and surfactants.