For years, scientists pointed fingers at amyloids twisted protein clumps as the bad guys behind memory loss in diseases like Alzheimer’s and Parkinson’s. The story always went: these misfolded proteins pile up, wreck brain cells, and take memories with them. But it turns out, that’s not the whole picture. New research shows that some of these very same proteins might actually help us hold onto our memories.
Also Read:India Sets the Record Straight on U.S. Trade Deal Update
A Fresh Look at Amyloids
Kausik Si and his team at the Stowers Institute for Medical Research dug into how the brain turns quick flashes of experience into long-lasting memories. Their study, published in the Proceedings of the National Academy of Sciences, found something unexpected. Specialized proteins called chaperones—think of them as molecular helpers—actually guide certain amyloids into useful shapes, not the destructive kind. These “functional amyloids” aren’t just harmless. They’re necessary for memory.
Chaperone proteins make sure other proteins fold the right way, so they can do their jobs. In fruit flies, which have surprisingly complicated brains for their size, the researchers focused on a chaperone they called “Funes.” When needed, Funes nudges amyloids to form in just the right brain spots, but only when the fly has a new experience to remember. More Funes meant flies remembered longer; block amyloid formation, and the flies simply couldn’t make long-term memories.
A Shift in Our Understanding of Memory
Most experts agree: to remember something for the long haul, the brain needs to make new proteins, especially at the synapses where neurons talk to each other. This is a key part of long-term potentiation basically, how the brain strengthens its wiring to lock in new experiences.
But until now, how these memory-building proteins actually do their work has been a mystery. Si’s study offers a rare peek at the process. It shows that certain proteins fold into stable forms that help anchor memories in place. And unlike the messy, uncontrolled amyloid clumps in dementia, these structures are precise and intentional.
Also Read:New Fixed Deposit Reporting Rules: What You Need to Know for 2026
Not All Amyloids Are Villains
People used to think amyloids were nothing but trouble sticky, tangled up, and deadly for brain cells. But now, researchers are drawing a clear line: there’s the harmful kind linked to disease, and there’s the functional kind, built on purpose, in response to learning. In Si’s study, these functional amyloids only showed up when chaperones like Funes gave the signal, and only when there was something worth remembering.
So, amyloids aren’t always bad. In the right place, at the right time, they might be crucial for stabilizing the brain changes that let us keep memories for good.
What This Means for Humans
Sure, the study used fruit flies. Their brains are tiny, but some of the same protein tricks play out in mammals too. Proteins like CPEB in mammals have already been linked to memory, and these new findings back up the idea that carefully controlled protein folding is a core part of how memory works.
This discovery could change how we think about diseases like Alzheimer’s as well. If both harmful and helpful amyloids use similar building blocks, then learning exactly what sets them apart could point us toward new ways to protect memory as we age or even fight off brain diseases.
