Effect of ambient polycyclic aromatic hydrocarbons and nicotine on the structure of Aβ42 protein

• Published in: Frontiers of environmental science & engineering 2023-02, Vol.17 (2), p.15-15, Article 15
• Main Authors: Kaumbekova, Samal, Torkmahalleh, Mehdi Amouei, Sakaguchi, Naoya, Umezawa, Masakazu, Shah, Dhawal
• Format: Article
• Language: English
• Subjects: Alzheimer's disease; amyloid; Benzo(a)pyrene; Biomarkers; Dynamic structural analysis; Earth and Environmental Science; Environment; hydrogen bonding; Hydrogen bonds; Hydrophobicity; Molecular dynamics; Molecular interactions; Monomers; Neurodegenerative diseases; Nicotine; Oligomers; Peptides; Phenanthrene; phenanthrenes; Pollutants; Polycyclic aromatic hydrocarbons; Protein structure; Research Article; risk; Secondary structure; β-Amyloid
• ISSN: 2095-2201; 2095-221X
• DOI: 10.1007/s11783-023-1615-2

Recent studies have correlated the chronic impact of ambient environmental pollutants like polycyclic aromatic hydrocarbons (PAHs) with the progression of neurodegenerative disorders, either by using statistical data from various cities, or via tracking biomarkers during in-vivo experiments. Among different neurodegenerative disorders, PAHs are known to cause increased risk for Alzheimer’s disease, related to the development of amyloid beta (Aβ) peptide oligomers. However, the complex molecular interactions between peptide monomers and organic pollutants remains obscured. In this work, we performed an atomistic molecular dynamics study via GROMACS to investigate the structure of Aβ 42 peptide monomer in the presence of benzo[a]pyrene, nicotine, and phenanthrene. Interestingly the results revealed strong hydrophobic, and hydrogen-bond based interactions between Aβ peptides and these environmental pollutants that resulted in the formation of stable intermolecular clusters. The strong interactions affected the secondary structure of the Aβ 42 peptide in the presence of the organic pollutants, with almost 50 % decrease in the α-helix and 2 %–10 % increase in the β-sheets of the peptide. Overall, the undergoing changes in the secondary structure of the peptide monomer in the presence of the pollutants under the study indicates an enhanced formation of Aβ peptide oligomers, and consequent progression of Alzheimer’s disease.