Researchers at the University of North Carolina at Chapel Hill have made a big breakthrough in drug delivery technology by developing a new platform that utilizes helical amyloid fibers.
These fibers are designed to unravel and release drugs when exposed to body temperatures, offering a promising new approach to treating diseases like Alzheimer’s.
In a study published in Nature Communications, the team shared insights into the structural dynamics of amyloid fibers, which are similar to those involved in the formation of Alzheimer’s disease.
This research not only sheds light on how such diseases develop but also suggests a potential method to counteract the harmful effects of amyloid deposits in the brain.
The research was led by Ronit Freeman at UNC-Chapel Hill, with collaboration from the Lynn lab at Emory University. They focused on the beta amyloid-42 peptide, a crucial component in the formation of amyloid plaques in Alzheimer’s patients.
By synthesizing various versions of this peptide in the laboratory, the researchers learned how to manipulate the assembly and twisting of these molecules.
Freeman highlighted the significance of their findings, stating, “The ability of these amyloid materials to be untwisted and degraded highlights potential for treatments modifying and subsequently reversing plaques found in Alzheimer’s, and other neurodegenerative diseases.”
The team discovered that the direction in which the amyloid fibrils twist is linked to different stages of disease progression. Their work suggests the possibility of a treatment that could alter the shape of amyloids and cause them to disintegrate.
The researchers utilized sophisticated spectroscopic methods to study how individual peptides interact with each other.
This allowed them to gather detailed information on how quickly the peptides assemble, the distances between them, their alignment, and the direction of their twist.
They also employed high-resolution electron and fluorescent microscopy to examine the structure of these materials at various temperatures.
One of the key findings was the role of the N-terminal domain of the peptide in determining the overall shape of the assembly, such as tubes, ribbons, or fibers. Modifications to the C-terminal end influenced whether the material would twist to the left or right.
By applying these design principles, the team was able to create peptides that could switch between left-handed and right-handed twists in response to temperature changes.
This ability to reverse the twist makes the material more susceptible to breakdown by natural enzymes, which is an advantageous property for drug delivery systems.
This groundbreaking research not only offers new insights into the mechanisms behind diseases like Alzheimer’s but also opens the door to innovative treatments that could potentially reverse the effects of these conditions.
If you care about Alzheimer’s, please read studies about Vitamin D deficiency linked to Alzheimer’s, vascular dementia, and Oral cannabis extract may help reduce Alzheimer’s symptoms.
For more information about brain health, please see recent studies about Vitamin B9 deficiency linked to higher dementia risk, and results showing flavonoid-rich foods could improve survival in Parkinson’s disease.
The research findings can be found in Nature Communications.
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