https://orcid.org/0000-0002-8651-9289
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Abstract
The truncated Aβ1 − 16 peptide containing the metal-binding domain is frequently used in in silico and experimental investigations because it is more soluble and thus more suitable for studies in solution and does not form amyloids. Several spectroscopic studies have shown that the metal binding of Aβ1 − 16 is very similar to that of the full-length Aβ1 − 42. However, since small changes can have a significant impact on aggregation, further experimental and theoretical are needed to elucidate the detailed structures of truncated and full-length Aβ. In this research, the binding of copper ion to the Aβ1 − 16 and Aβ1 − 42 has been studied by molecular dynamics simulation method. To investigate the effect of copper ion on beta-amyloid peptide structure, the simulations were repeated in the copper and zinc ions, copper and iron binary system, and the copper, zinc and iron ions ternary system. The conformation factor was calculated to calculate the binding affinity of copper ion to beta-amyloid peptide residues. The results showed that the initial 16 residues of the beta-amyloid peptide have high binding affinity for copper ions, and histidine 13 and histidine 14 have significantly higher binding affinity for copper ions in all studied systems. Zinc and iron ions were found to reduce the conformational factor of peptide residues in binding to copper ions, and the aggregation tendency was lower in the truncated structure. The SASA results suggest that the side chains of peptide residues are more affected by shortening and the presence of ions.
Communicated by Ramaswamy H. Sarma
Disclosure statement
No potential conflict of interest was reported by the author(s).