New insights into how cell membranes influence peptide development in Alzheimer’s disease

Researchers wanted to better understand how cell membranes in the body influence the structure of peptides (molecules made up of amino acids) and their aggregation. To do this, they used an ly controllable model system.

Lead author Dr. Torsten John, who received his PhD in Leipzig under Professor Bernd Abel and is now a researcher at the Massachusetts Institute of Technology (MIT) in the United States, explains: effects of stress It triggers oxidative processes in the body and changes the chemical composition of membranes. In our experiments, we compared the effect of oxidized membranes to unmodified membranes. ”

Scientists use biophysical laboratory experiments and computer simulation To better understand peptide aggregation. “Computer simulation molecular dynamics simulationprovides molecular insight into the mechanisms of interaction between membranes and peptides,” explains Professor Abel.

it was already known film Composition plays an important role in peptide aggregation. However, little research has been done on the role of the oxide film. Researchers found that the effects differed between peptides. One of the studied peptides associated with Alzheimer’s disease (Aβ40) aggregated faster in the presence of all membranes.

In contrast, aggregation of another peptide (uperin 3.5) was completely prevented in the presence of the same amount of oxide film. According to Abel, “Depending on the peptide’s properties, such as its charge, adsorption to the membrane changes and the strength of the effect changes. When peptides accumulate on the membrane surface, they accelerate their assembly and aggregation. But when the attractive force is so strong that it turns the structure into a spiral, it can no longer clump together.”

Scientists deliberately selected peptides that aggregate similarly but have different origins for their study. Aβ40 is known to be deposited in the brains of Alzheimer’s disease patients, while uperin 3.5 was the first antimicrobial peptide discovered in the Australian toad species. Previously, a team of researchers led by Professor Lissandra L. Martin of Monash University, Australia, reported a possible link between peptide aggregation in cells. neurodegenerative disease and antimicrobial properties of peptides.

Research published in journals chemical sciencefurther discusses the functional role of amyloid peptides.

For more information:
Torsten John et al., Lipid oxidation controls near-membrane peptide self-assembly through a surface attraction mechanism. chemical science (2023). DOI: 10.1039/D3SC00159H

provided by
Leipzig University

Quote: New Insights into How Cell Membranes Affect Peptide Occurrence in Alzheimer’s Disease (March 6, 2023), March 6, 2023 at https://phys.org/news/2023-03 -insights-cell-membranes-peptides-alzheimer. html

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