ArticleJournal of molecular modeling2019
Amyloid beta oligomers: how pH influences over trimer and pentamer structures?
Article in Journal of molecular modeling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Effect of a Low Electrostatic Environment on the Helical Structures of Peptides and Proteins Using Flexible Water Models: An In Silico Study.ACS omega · 2025Article
- A Hairpin Motif in the Amyloid-β Peptide Is Important for Formation of Disease-Related Oligomers.Journal of the American Chemical Society · 2023Article
- Silver cluster doped graphyne (GY) with outstanding non-linear optical properties.RSC advances · 2022Article
- Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity.Applied and environmental microbiology · 2021Article
- Nerve Growth Factor Peptides Bind Copper(II) with High Affinity: A Thermodynamic Approach to Unveil Overlooked Neurotrophin Roles.International journal of molecular sciences · 2021Article
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Authors and funding
5 authors.
Funding
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Abstract
The aggregation of proteins in the brain is one of the main features of neurodegenerative diseases. In Alzheimer's disease, the abnormal aggregation of Aβ-42 is due to intrinsic and extrinsic factors. The latter is due to variations in the environment, such as temperature, salt concentration, and pH. We evaluated the effect of protonation/deprotonation of residues that are part of trimeric and pentameric oligomers at pH 5, pH 6, and pH 7. Molecular dynamics simulation at 200 ns in the canonical ensemble was implemented. The results have revealed that histidine, glutamic acid, and aspartic acid residues showed a protonation/deprotonation effect in oligomers. The root mean square deviation analysis was used to analyze the structural stability at different pHs. We found an increase in hydrophobicity in the side chains of the trimer, while in the pentamer, the structural instability of a compact structure at pH 5 caused the hydrophobic core to open, revealing the hydrophobic region to the environment. At this point, we believe that conformational changes mediated by pH are essential in the aggregation of Aβ-42 oligomers.
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Registered trials
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