Duke Chemists Isolating Individual Molecules Of Toxic Protein In Alzheimer's, Parkinson's Disease ( fully understood he said. When y...)

Duke Chemists Isolating Individual Molecules Of Toxic Protein In Alzheimer's, Parkinson's Disease

fully understood," he said.

"When you start a normal reaction, molecules are free in solution so they interact with each other randomly," Akhremitchev said. "If you want to dissect the process, you would rather want to study interactions individually."

Thus, the Duke chemists capture individual monomers at the end of long chained polyethylene glycol molecules. They then attach one such tethered monomer to a microscope slide and the other to the AFM microscope tip. They can then bring the isolated and suspended molecules together to study how and whether they interact.

The Duke researchers study these interactions by retracting the tip of their AFM, which can measure changes in force at the atomic scale. Pulling back the tip can induce a measurable tug on the chemical bonds that hold together the two elevated monomers.

By pulling on such bonds, the Duke scientists can deduce how much energy was required to bring the molecules together. Then, using their knowledge of protein chemistry, they can develop hypotheses about how those particular monomers might, or might not, be involved in the evolution of fibrils, They can thus develop a better understanding of amyloid aggregation.

The scientists are also seeking the precise point during fibril formation when interactions between monomers become irreversible. Defining that point is important because "the fibrils are virtually indestructible once formed," he said.

"How all these monomers interact to form these amyloid fibrils is just not known at this point," said Akhremitchev. "And that is why it is such a great challenge. That's what we want to learn."

Source:Duke University

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