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Scientists thought this peptide was harmless. A new discovery could rewrite Alzheimer’s research
Lab research suggests the little-studied peptide can form amyloid clumps and may damage neurons, but its role in Alzheimer’s patients remains unproven.
For decades, the search for an Alzheimer’s treatment has centered on one major culprit—amyloid beta. But now, a University of California Santa Cruz chemist argues that scientists may have overlooked a closely related peptide long dismissed as harmless in their research.
In a commentary published in the peer-reviewed journal ChemBioChem, Jevgenij Raskatov, PhD, professor of chemistry and biochemistry at UC Santa Cruz, highlights new research which suggests that the lesser-known peptide, P3, can form the same clumps and fibrils as amyloid beta, the target of most Alzheimer’s drug development. P3 may also interact with amyloid beta, influencing how it builds up and how toxic it becomes.
These findings ultimately suggest that P3 may be contributing to the nerve cell damage associated with Alzheimer’s disease.
“The P3 peptide is, most likely, not the innocent bystander it was commonly thought to be. There’s still more research to be done. But this could turn Alzheimer’s research on its head,” Raskatov said in a release. Instead, he’s proposed to rename it amyloid alpha, or Aα.
What P3 is and why scientists dismissed it
Amyloid beta comes from a large protein embedded in cell membranes called the Amyloid Precursor Protein (APP). Two enzymes, β-secretase and γ-secretase, cut the protein in a sequence, freeing amyloid beta fragments of different lengths.
Previously, researchers have focused on two of those fragments, Aβ40 and Aβ42. Aβ42 has been reviewed the most because it is especially prone to sticking together and clumping into toxic aggregates.
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But unlike amyloid beta, P3 forms when APP is processed through a different sequence of molecular cuts. The enzyme α-secretase acts first, and then γ-secretase, and P3 forms when alpha-secretase does. Researchers previously assumed that P3 stayed dissolved and didn’t clump, nor was it presumed to be toxic. But Raskatov did not believe that these assumptions were ever adequately tested.
“We were looking at the peptide sequence and noticed that two-thirds of charged residues were located in the N-terminal segment of A-beta that was missing in A-alpha,” Raskatov told Inc. Since charged residues help a molecule dissolve in water, P3’s lack of them casts doubt on the idea that it simply stays in solution, he said.
The evidence that P3 may not be harmless
Over the past five years, Raskatov’s team published three studies showing that P3 forms amyloid aggregates faster than amyloid beta and may be toxic to neurons, though less so. An independent group in the United Kingdom has since confirmed the findings, according to the release. Though, it is important to note that this new paper is a commentary, not a study. The research it draws on was done in the lab, and whether P3 contributes to Alzheimer’s in patients still remains unproven.
Raskatov told Inc. that it is impossible to know exactly what the narrow focus on amyloid beta has cost the field, but it has likely been damaging.
“Focusing on a subset of the problem instead of the whole picture is likely to be limiting in ways that are hard to predict,” Raskatov told Inc. “How can you rationally solve a problem that you don’t understand?”
What P3 could mean for Alzheimer’s treatments
Targeting multiple amyloid species might change treatment strategy, he said, especially given how common P3 may be. Raskatov noted that alpha-secretase processing appears roughly twice as prevalent in neurons as beta-secretase processing.
“This means that A-alpha is likely the main product of APP processing and not A-beta,” Raskatov said, adding that “only more experiments can determine what exactly that means.”
This post originally appeared at inc.com.
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