Beta-amyloid peptides, protein pieces that frame normally in the brain and cluster into plaques in Alzheimer’s disease patients, are believed to be in charge of neuron death. Scientists are yet to find out how these substances kill cells.
According to the latest study by the Purdue University, beta-amyloids are responsible for killing the cells by boring holes into them. The study suggests that the beta-amyloid forms the pores that kill neural cells in patients afflicted with Alzheimer’s disease.
Scientists used computer simulations to observe how antimicrobial peptides produced by insects protect them against harmful microorganisms. They found that the antimicrobial peptides frame aggregates and bore into the cells of foodborne pathogens, making pores that enable intracellular liquid to release, along these lines, slaughtering the phones and lightening the risk of nourishment harming. Since proteins and peptides are ordinary constituents of all sustenances, that work holds guarantee for making “green” nourishment security items, for example, showers for new delivery and bundling films.
Ganesan Narsimhan, professor in the Department of Agricultural and Biological Engineering knew that antimicrobial peptides had to form small clusters in order to kill pathogenic cells, and he noticed that while beta-amyloid alone does not cause cell death, the formation of beta-amyloid aggregates could. He set out to determine whether beta-amyoild and microbial peptides functioned in similar ways to kill cells.
Scientists especially focused on the Aβ 1-42. Then in collaboration with Xiao Zhu, a senior research scientist for Information Technology at Purdue Research Computing, Narsimhan’s research group performed computer simulations showing that a single Aβ 1-42 peptide had no effect on neural cells, but in groups of three or five, called oligomers, they are able to penetrate the cell membrane and form small pores and kill the neural cells.
Narsimhan said, “The aggregation of these peptides is a precursor to penetration of the neural cell, leading to the formation of a pore. This demonstrates that formation of an aggregate is an essential step in the penetration and formation of pores leading to neural cell death. That’s what happens in Alzheimer’s disease.”
The work suggests that neural cell death in Alzheimer’s disease could be slowed or stopped with therapies that inhibit the formation of these toxic beta-amyloid peptide aggregates.
Narsimhan said, “The cure or therapy to Alzheimer’s and other neurodegenerative diseases may lie in preventing the formation of oligomers in the fluid within the brain.”
The findings were published as the cover story in the March issue of the journal Physical Chemistry Chemical Physics.