Quantum turkey? Tryptophan displays bizarre trait that may protect the brain from diseases

WASHINGTON — Can eating turkey play a role in how quantum fiber optics protects the brain against neurodegenerative diseases? Tryptophan, an amino acid best known as the culprit behind your post-Thanksgiving nap, is joining forces in a way that could revolutionize our understanding of how biological systems interact with ultraviolet light. Howard University researchers have discovered that when trillions of tryptophan molecules come together in specific protein structures, they exhibit incredible UV-responsive properties, acting as tiny antennas that can capture and funnel UV energy with unprecedented efficiency.

At the heart of this discovery, published in The Journal of Physical Chemistry, are the tryptophan “mega-networks” — vast arrays of tryptophan molecules strategically positioned within protein structures like microtubules, the microscopic scaffolding that gives our cells shape and helps them divide. These networks, some containing over 100,000 tryptophan molecules, absorb UV light and then re-emit it in a highly coordinated fashion, a phenomenon known as superradiance.

Superradiance is a bit like a stadium wave at a sporting event. When excited, each tryptophan acts like an eager fan, absorbing a photon and then passing it along to its neighbors in a synchronized emission of light. This collective behavior allows the network to process UV energy much more efficiently than any one tryptophan molecule could alone. The researchers predict that in certain geometries, like the barrel-shaped centriole structure found in most animal cells, tryptophan superradiance could enhance UV absorption by a factor of 4,000!

However, what really sets these mega-networks apart is their resilience. The team found that the superradiant properties persisted even in the face of significant disorder and disruption, such as the thermal noise present in cells at room temperature. This robustness suggests that tryptophan’s UV superpowers aren’t just a fluke but a feature that has been honed over eons of evolution.

Large quantum optical networks of tryptophan in protein architectures – the kinds found in mammalian brains, but also in all eukaryotes and even in some bacteria – influence their collective response to an ultraviolet light stimulus
Large quantum optical networks of tryptophan in protein architectures – the kinds found in mammalian brains, but also in all eukaryotes and even in some bacteria – influence their collective response to an ultraviolet light stimulus. These lattices of tryptophan, an amino acid that strongly absorbs and emits in the ultraviolet, are scaffolded within much larger protein assemblies that self-organize in neurons, centrioles, cilia, and flagella. The existence of such a cooperative and ultrafast optical response in cytoskeletal filaments, neuron fibers, and other cellular organelles reveals their ability to process electromagnetic energy and information in unanticipated ways. Life has thus found a way to exploit molecular symmetries to enhance collective quantum optical behaviors, which are robust to warm and wet environments. (CREDIT: Quantum Biology Laboratory: Nathan Babcock and Philip Kurian)

“I believe that our work is a quantum leap for quantum biology, taking us beyond photosynthesis and into other realms of exploration: investigating implications for quantum information processing, and discovering new therapeutic approaches for complex diseases,” says study author Dr. Philip Kurian, principal investigator and founding director of the Quantum Biology Laboratory at Howard University, in a media release.

So, why does all this matter? For starters, it could help explain how organisms across the tree of life perceive and respond to UV light. Many proteins involved in UV detection, DNA repair, and circadian rhythms are studded with tryptophans, hinting that these amino acid arrays might act as built-in UV sensors and energy conduits. Superradiance could be life’s way of making the most of the high-energy photons that constantly bombard us.

There are also tantalizing medical implications. Howard researchers found evidence that tryptophan mega-networks may play a photoprotective role, allowing proteins to efficiently disperse potentially damaging UV energy rather than letting it wreak havoc on delicate cellular structures. This could be especially relevant for understanding neurodegenerative diseases like Alzheimer’s, where the accumulation of protein aggregates is a key factor.

However, the most exciting applications may lie in the realm of bioengineering. Imagine if we could harness tryptophan’s superradiant properties to create ultra-efficient, nanoscale UV light harvesters or even “light wires” that could guide photons through microscopic circuits. The possibilities are endless, and they all start with a deeper appreciation of the quantum magic happening right under our noses (or, more accurately, in our noses).

“It’s a beautiful result,” says study author Majed Chergui, a professor at the Swiss Federal Institute of Technology (EPFL), who led the experimental team. “It took very precise and careful application of standard protein spectroscopy methods, but guided by the theoretical predictions of our collaborators, we were able to confirm a stunning signature of superradiance in a micron-scale biological system.”

There’s still much work to be done to turn these quantum insights into tangible technologies. The researchers stress that their findings, while groundbreaking, represent just the first steps in a new field they’ve dubbed “quantum biology.” But if one thing is clear, it’s that we’ve only begun to scratch the surface of what our cells’ trillion-strong tryptophan tag teams can do.

“This photoprotection may prove crucial in ameliorating or halting the progression of degenerative illness,” concludes Kurian. “We hope this will inspire a range of new experiments to understand how quantum-enhanced photoprotection plays a role in complex pathologies that thrive on highly oxidative conditions.”

StudyFinds’ Matt Higgins contributed to this report.

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