Collaborative research by the University of Tokyo and RIKEN Center for Biosystems Dynamics Research has led to the development of a new method for simultaneously synthesizing all transfer RNA (tRNA) required for protein synthesis in a reconstituted translation system in vitro.

The findings are published in the journal Nature Communications.

Currently, humans rely on living organisms (bacteria, yeast, plants, and animals) for the production of pharmaceuticals and food. However, living organisms are susceptible to environmental changes, breeding improvements require time, and achieving precise control is difficult. If we could build artificial systems possessing the ability to regenerate themselves, like living organisms, we could realize stable production systems that are precisely designed and controllable, like industrial products, and are unaffected by environmental factors.

Developing self-regenerating artificial molecular systems, that is, systems that create themselves, requires synthesizing the protein synthesis system itself in a test tube using that very system. Ichihashi and his research group have already achieved world-first success in the sustained reproduction of all 20 enzymes (aminoacyl-tRNA synthetases) essential for the protein synthesis system.

However, the protein synthesis mechanism requires at least 21 types of tRNA, which presents a significant technical barrier. Therefore, in this study, they developed a novel method (the tRNA array method) to synthesize all 21 types of tRNA simultaneously within the tRNA-omitted protein synthesis system.

In this method, all tRNAs corresponding to the 20 amino acids are encoded as genes within a single DNA (plasmid). From this, the tRNAs are transcribed collectively and then separated into individual tRNAs using the HDV ribozyme and RNase P. They can then be used directly to translate any desired gene.

This research represents a significant step toward realizing an artificial molecular system with self-reproducing capabilities. By adding further necessary genes to this system, it is anticipated that this will lead to the development of material production platforms with higher design flexibility and controllability than those of biological systems in the future.

Furthermore, this tRNA synthesis method is expected to greatly simplify genetic code modification, contributing to the development of artificial proteins and peptides that incorporate non-natural amino acids.

A new tool greatly improves scientists’ ability to identify and study proteins that regulate gene activity in cells, according to research led by Weill Cornell Medicine investigators. The technology should enable and enhance investigations in both fundamental biology and disease research.

The activity of a gene is often regulated—switched on, sped up, slowed down, switched off—by one or more proteins that bind to DNA to exert their effect. However, identifying these DNA-binding proteins has been challenging due to the lack of a precise method. In their study, reported Sept. 29 in the Proceedings of the National Academy of Sciences, the researchers developed a molecular tool that can be targeted to virtually any spot on the genome to capture any protein that lies nearby, allowing the protein’s identification. The team demonstrated the power of their new tool by using it to discover new protein regulators of human stem cell-related genes.

“We expect this to be useful as a very general laboratory tool, and we already plan to use it for research on specific disorders, including type 1 diabetes,” said study co-senior author Dr. Shuibing Chen, the Kilts Family Professor of Surgery, director of the Center for Genomic Health and a member of the Hartman Institute for Therapeutic Organ Regeneration at Weill Cornell Medicine.

The study’s other co-senior author was Dr. Peter Schultz, the Skaggs Presidential Chair of Chemistry and CEO and President at Scripps Research.

The new tool, which the researchers have dubbed SCOPE, has two key elements. One is a protein incorporating a “guide RNA” that can be designed to bind to virtually any site on the genome. The other key element is a special amino acid—a building block of proteins—that when hit with a flash of ultraviolet light, will form a strong and enduring bond to any protein in close proximity. Researchers using the tool can relatively easily isolate the resulting SCOPE-bound protein and identify it using a standard set of methods called mass spectrometry.

The special amino acid used in SCOPE has the further remarkable property that it is based on an amino acid found only in some ancient, single-celled microorganisms called archaea. Because of this evolutionary distance, it has essentially zero natural reactivity with other amino acids in mammalian and even bacterial cells—it becomes reactive only when exposed to UV light.

“This reduces the chances of unwanted interactions between the SCOPE tool and other proteins, which effectively gives SCOPE a high sensitivity, enabling it to detect proteins that are DNA-bound only weakly and/or transiently,” said study first author Dr. Jiajun Zhu, a postdoctoral researcher in the Chen laboratory.

The use of the special amino acid, known as AbK, was pioneered by the Schultz laboratory, where Dr. Chen did her graduate research, in work aimed at developing other laboratory tools.

The SCOPE tool is meant to be engineered into the DNA of any cell type, including stem cells; it thus assembles and operates internally in the cell to bind proteins at any genomic site specified by the guide RNA.

In their study, the team used SCOPE to illuminate the DNA-binding roles of three proteins in human embryonic stem cells. They showed that two of the proteins work to maintain these stem cells in their immature, stem-like state, while the third helps induce the differentiation of the stem cells into more mature cell types.

Drs. Chen and Zhu and their colleagues now hope to use SCOPE to uncover gene-regulating proteins in other cell types and in specific disease contexts, including cardiomyocytes in heart arrhythmias, insulin-producing pancreatic cells in type 1 diabetes, and neurons in neurodegenerative disorders.

A new way to potentially control when drugs are active or inactive in the body is introduced in a study reported Sept. 24 in Nature. The research showed that, instead of controlling how tightly proteins bind to partner molecules, scientists can now directly control how long they stay bound. This advance has broad implications for developing safer medicines.

“One way to control a medicine is through dose. We’ve added a second lever by designing molecules that can be switched off rapidly, even after they’ve taken full effect,” said senior author David Baker, a professor of biochemistry at the University of Washington School of Medicine and a Howard Hughes Medical Institute investigator.

Proteins often cling to other molecules to drive immune signaling, metabolism and more, but this stickiness can be problematic for medicines. For example, once an antibody drug begins to stimulate the immune system, it can be difficult to halt its activity if dangerous side effects emerge.

To address this concern, a team from the Baker Lab used computers to create custom proteins that latch onto target molecules. A separate molecule called an effector could then be added to force the bound complex into a strained configuration, causing it to fall apart.

“In one experiment, interactions that would otherwise last for 20 minutes completely broke apart in just 10 seconds. I was so surprised by that speed-up that I had to repeat my measurements a few times before I could really believe it,” said lead author Adam Broerman, a chemical engineering Ph.D. student training at the UW Medicine Institute for Protein Design.

His team applied this technology to interleukin-2 (IL-2), a powerful immune protein that has long been investigated as a cancer therapy but is notorious for toxic side effects. They created a switchable version of IL-2 that activates human immune cells in a lab dish and, with an added effector, silences them on demand.

This new form of control could make future cancer immunotherapies more tunable, thereby potentially protecting patients from runaway side effects, or allowing doctors to administer high-dose, short-duration treatments to achieve better cancer-killing results.

The same technique was used to create improved molecular sensors. In the study, a switch introduced into a light-emitting enzyme yielded a bright signal that could be toggled in seconds. This advance was adapted into a rapid coronavirus sensor that responds about 70 times faster than previous protein-based tests for SARS-CoV-2. The same approach might be used to create rapid sensors for disease markers, environmental pollutants and other chemicals.

The Piehler Lab at Osnabrück University and the Stoll Lab at the University of Washington School of Medicine contributed biophysical measurements, the Garcia Lab at Stanford University contributed cell measurements, and the Zuckerman Lab at Oregon Health & Science University contributed molecular dynamics simulations.

Cruciferous vegetables like radish, broccoli and kale offer significant health benefits, especially when they are consumed as microgreens, or as young seedlings harvested early. The little plants contain nutrients such as vitamins; minerals; bioactive antioxidants, like polyphenols; and glucosinolates, which have cancer-fighting potential.

But microgreens are highly perishable and lose nutritional value quickly. In an effort to boost the impact and accessibility of microgreens, a team of researchers at Penn State conducted a study of how hot air drying—a cheap and relatively easy preservation technique—affects the availability of key nutrients and plant compounds that benefit health.

“Microgreens increasingly are popular due to their high concentrations of health-promoting compounds, but their benefits have been limited because they’re highly perishable, lasting only one to two days at room temperature and seven to 14 days with refrigeration,” said team leader Joshua Lambert, professor of food science in the College of Agricultural Sciences, senior author on the study.

“That limits their use, increases costs, and leads to food waste—especially in places without good refrigeration. So, there’s a clear need for preservation methods that keep nutrients intact.”

In findings published in the Journal of Food Science, the researchers reported that radish microgreens, no matter at what temperature they were dried, retained a significant portion of nutrients.

From their drying experiments, the team specifically found that radish microgreens retained 91% of their total phenolic content—antioxidants—after drying at 113°F (F) and 79% after drying at 149 F. Those dried at 203 F retained 100%. Glucoraphenin—a specific glucosinolate with potential anti-cancer properties—was stable after drying at 113 F and 149 F and was retained at 78% after drying at 203 F. Vitamins B1 and B9 were stable at all drying temperatures. Vitamin B2, B3 and C were retained by up to 65%, 64% and 37% respectively with heat exposure.

Using simulated digestion—a laboratory process that recreates the digestive environment of the human gastrointestinal tract to study how food and other substances are broken down and nutrients are absorbed—the researchers also measured the effects of drying methods on bioaccessibility, or how well nutrients can be absorbed by the body after digestion. They found that total phenolic content and vitamins B1, B3, B9 and C had bioaccessibility ranging from 13% to 68%, with no major differences across the drying methods.

Vitamin B2 was more bioaccessible after being dried at 149°F than at other temperatures. Glucoraphenin and anthocyanins—polyphenols that can also act as antioxidants, offering potential health benefits such as supporting cardiovascular and immune health—could not be detected after simulated digestion, meaning they broke down or became unmeasurable, according to Lambert.

Metabolomic analysis—the comprehensive study of small molecules, or metabolites, in cells and tissues—showed that different drying methods led to different overall chemical profiles, noted study first author, Marjorie Jauregui, a pilot plant research technologist at Penn State. Glucosinolates and flavonoids—a class of plant pigments that provide various health benefits—were major contributors to these differences, she explained.

“Hot air drying, even at higher temperatures, can be an effective way to preserve nutrients in radish microgreens, especially for making powders that can be used in food products,” Jauregui said. “While some nutrients are lost, others remain stable and, overall, hot air drying is a practical and promising postharvest method.”

As microgreens are increasingly promoted for healthy eating, understanding how to preserve their nutrients without expensive equipment is essential, Lambert noted, adding that results from this study could help in making nutrient-dense microgreen powders more accessible and sustainable, especially for areas lacking refrigeration or advanced drying technology.

“Freeze-dried microgreens require expensive, specialized equipment to produce,” he said. “Hot air drying is more practical, especially in low-resource areas, but we need to fully understand how different drying temperatures affect key nutrients and phytochemicals—plant compounds that provide health benefits. These results are more than a good start.”

A research team led by Prof. Wang Yanli from the Institute of Biophysics of the Chinese Academy of Sciences has revealed the structure and mechanism of a highly active Type II-D Cas9, offering a promising new tool for genome editing. The study was published on August 11 in Nature Communications.

Cas9 is the hallmark protein of Type II CRISPR-Cas systems, with Streptococcus pyogenes Cas9 (SpCas9) the most widely used for its high cleavage efficiency and robust genome-editing performance. However, its large molecular weight limits delivery through adeno-associated virus (AAV) vectors. Therefore, identifying naturally occurring or engineered Cas9 variants with smaller molecular size yet comparable cleavage activity has become essential.

In this study, the researchers focused on a Type II-D Cas9 derived from a Nitrospirae bacterium (NsCas9d), which consists of only 762 amino acids. Using metagenomic datasets, the researchers identified the CRISPR repeats and spacers associated with NsCas9d and designed a corresponding sgRNA.

In vitro cleavage assays showed that NsCas9d requires at least a 20-nt pairing between the substrate dsDNA and sgRNA to achieve robust dsDNA cleavage activity comparable to that of SpCas9.

PAM depletion assays combined with high-throughput sequencing revealed that NsCas9d recognizes the 5′-NRG-3′ PAM sequence, with the 5′-NGG-3′ PAM exhibiting the highest cleavage efficiency in vitro.

The researchers further resolved the cryo-EM structure of the NsCas9d-sgRNA-dsDNA ternary complex at 2.86 Å resolution, marking the first report of a complete HNH and RuvC domain structure for a Type II-D Cas9.

In the structural model, the dsDNA PAM sequence is accommodated within a positively charged binding channel formed by the PI and WED domains. Importantly, NsCas9d generates 3-nt 5′ overhangs as cleavage products, a sticky-end feature that can improve the efficiency and predictability of DNA repair processes during gene editing operations such as insertions.

This study not only deepens our understanding of Cas9 evolution and molecular mechanisms but also highlights the potential of NsCas9d as a compact and efficient tool for genome editing applications.

The dodo has been extinct for more than 300 years, but that isn’t stopping Dallas’ Colossal Biosciences from trying to resurrect the 3-foot-tall, flightless bird.

On Sept. 17, the “de-extinction” biotech company announced it cleared an early hurdle by growing primordial germ cells—the precursors to eggs and sperm—from the rock dove, also known as the common pigeon.

Colossal said the next phase is to gene-edit primordial germ cells from the Nicobar pigeon, the dodo’s closest living relative. The Nicobar genome will serve as the scaffold for reconstructing a dodo-like genome. The company said it has established a breeding colony of Nicobar pigeons in Texas and is working to develop that bird’s primordial germ cells for editing.

“Our avian team’s breakthrough in deriving culture conditions that allow pigeon primordial germ cells to survive long-term is a significant advancement for dodo de-extinction,” Ben Lamm, CEO and co-founder of Colossal Biosciences, said in a press release.

“This progress highlights how Colossal’s investment in de-extinction technology is driving discovery and developing tools for both our de-extinction and conservation efforts.”

Cloning birds is trickier than cloning mammals. In mammals, scientists take an unfertilized egg, remove its nucleus and replace it with the nucleus from a donor body. Birds’ large, opaque eggs are laid after embryos begin developing, which complicates the approach.

Scientists have previously been able to culture and gene-edit primordial germ cells of chickens and geese, a technique that has been used to create a chicken fathered by a duck. But the “recipe has not worked on any other bird species tested, even closely related species like quail,” Anna Keyte, Colossal’s avian species director, said in the press release.

Colossal said it screened more than 300 “recipes” before landing on one that kept pigeon primordial germ cells growing for 60 days. The methods and data were posted on the preprint server bioRxiv and have yet to be peer-reviewed.

Colossal plans to inject the gene-edited Nicobar germ cells into chicken embryos. The chickens would grow up with pigeon-making cells in their ovaries or testes, acting like surrogates. In that way, a chicken could lay an egg that hatches a pigeon and, after additional gene edits, potentially a dodo-like bird.

Colossal aims to rewild the resurrected dodo in Mauritius, an island country off the coast of East Africa where the birds were endemic before going extinct in the 17th century.

The development follows the company’s announcement in July to bring back the giant moa, a 10-foot-tall, flightless bird that vanished from New Zealand roughly 600 years ago.

Beth Shapiro, Colossal’s chief science officer, called the ability to grow the primordial germ cells a “transformative tool for avian conservation.”

“By developing these protocols,” Shapiro said in the press release, “we’re establishing crucial biobanking capabilities and opening new possibilities for genetic rescue of endangered species.”

Some endangered birds include the Mauritian pink pigeon, which is expected to go extinct in the next 50 to 100 years due to inbreeding.

Colossal is also pursuing de-extinction projects for mammals including the woolly mammoth and Tasmanian tiger. In April, the company announced the birth of three dire wolves, modern canids engineered to resemble the long-extinct species popularized by HBO’s Game of Thrones.

Critics counter that true resurrection isn’t possible. Without intact genomes, they say, the best outcome is a genetically modified proxy or hybrid.

For decades, gene-editing science has been limited to making small, precise edits to human DNA, akin to correcting typos in the genetic code. Arc Institute researchers are changing that paradigm with a universal gene editing system that allows for cutting and pasting of entire genomic paragraphs, rearranging whole chapters, and even restructuring entire passages of the genomic manuscript.

In a paper published in the journal Science, the research team shows how bridge recombinase technology can be applied to human cells. The advance allows scientists to manipulate large genomic regions, testing up to a million base pairs in length, by inserting new genes, deleting entire gene clusters, or inverting regulatory sequences.

“Bridge recombinases could transform how we create genetic therapies by offering one versatile medicine per patient population instead of thousands of individual treatments,” says senior author Patrick Hsu, an Arc Institute Core Investigator and University of California, Berkeley bioengineering faculty member.

“With the ability to move and reshape entire genetic regions, we can engineer biology at the scale that evolution operates upon and apply those capabilities to solving complex diseases.”

Bridge recombinases were discovered from parasitic mobile genetic elements that hijack bacterial genomes for their own survival.

Presented in 2024 in the journal Nature, the same team found these elements encode both a new class of structured guide RNA, which they named a “bridge RNA,” and a recombinase enzyme that rearranges DNA.

Hsu and his colleagues repurposed this natural system by reprogramming the bridge RNA to target new DNA sequences, creating the foundation for a new type of precise gene editing tool they called bridge recombinases.

“What’s different about our new paper is not only are we able to show insertion into the human genome but we’re also showing quite efficiently the excision and inversion of genomic sequences in a programmable way,” says lead author Nicholas Perry, an Arc scientist in the Hsu Lab who also conducted this research as a UC Berkeley Ph.D. student.

“The applications of this platform are particularly exciting and could apply broadly across many kinds of scientific projects.”

Starting with 72 different natural bridge recombinase systems isolated from bacteria, the team found that about 25% showed some activity in human cells, but most were barely detectable. Only one system, called ISCro4, showed enough measurable activity to enable further optimization.

They then systematically improved both the protein and its RNA guide components, testing thousands of variations until they achieved 20% efficiency for DNA insertions and 82% specificity for hitting intended targets in the human genome.

While CRISPR uses a single guide RNA to target one DNA location, bridge RNAs are unique because they can simultaneously recognize two different DNA targets through distinct binding loops. This dual recognition enables the system to perform coordinated rearrangements such as bringing together distant chromosomal regions to excise genetic material or flipping existing sequences in reverse orientation.

The system acts as molecular scaffolding that holds two DNA sites together while the recombinase enzyme performs the rearrangement reaction.

As a proof-of-concept, the researchers created artificial DNA constructs containing the same toxic repeat sequences that cause progressive neuromuscular decline in Friedreich’s ataxia patients.

While healthy individuals carry fewer than 10 sequential copies of a three-letter DNA sequence, people with the disorder can harbor up to 1,700 copies, which interferes with normal gene function.

The engineered ISCro4 successfully removed these repeats from the artificial constructs, in some cases eliminating over 80% of the expanded sequences.

“Since disease severity correlates with repeat length, any amount of excision, whether it’s a perfectly healthy genotype or not, has the potential to improve patient symptoms,” Perry says.

“Bridge recombinases could apply to any heritable disease that results from expansions, and because we only need to deliver RNA molecules rather than proteins or DNA to make it work inside human cells, the approach could be much simpler to implement and scale.”

The team also demonstrated that bridge recombinases could replicate existing therapeutic approaches by successfully removing the BCL11A enhancer, the same target disrupted in an FDA-approved sickle cell anemia treatment. And because bridge recombinases can move massive amounts of DNA, the technology could also help model the large-scale genomic rearrangements associated with cancers.

The investigators are now working to expand the platform’s capabilities, including testing bridge recombinases in clinically relevant immune cells and stem cells, developing therapeutic delivery methods, and engineering variants that can handle DNA segments larger than a million base pairs. They also plan to explore applications in plant genetics and synthetic biology.

Scientists from James Cook University have developed a new computer tool that reveals layers of gene activity that were previously invisible, opening fresh possibilities for understanding health and disease.

The tool, called ScIsoX, looks at tiny variations in how genes are read inside individual cells—known as isoforms. These isoforms can change how a cell behaves, but most existing methods overlook them.

“Genes are like songs, and isoforms are the different remixes,” said Thaddeus Wu, postdoctoral fellow at the College of Science and Engineering and lead author of the work published in the journal Genome Biology.

“ScIsoX lets us hear the full playlist, not just the main track.”

By analyzing single cells from real-world datasets, ScIsoX uncovered patterns of gene activity that could help researchers better understand conditions like cancer, neurological disorders and immune diseases.

The software is free for scientists worldwide on GitHub.

Steviol glycosides, natural sweeteners extracted from Stevia rebaudiana, are widely used as sucrose substitutes due to their high sweetness and low caloric value. Among them, Rebaudioside M (Reb M) is regarded as a next-generation, high-value steviol glycoside product because of its intense sweetness and superior taste profile. However, the natural abundance of Reb M in Stevia is extremely low.

Efficient biosynthetic methods are needed to meet market demand. Until now, the key enzyme catalyzing the conversion of Rebaudioside D (Reb D) to Reb M in the biosynthetic pathway has not been identified, and it is generally assumed to be UGT76G1. However, UGT76G1 exhibits strict regioselectivity for the C13 position of steviol glycosides, while its catalytic activity at the C19 position is very weak.

In a study published in the Proceedings of the National Academy of Sciences on September 17, a team led by Prof. Yin Heng from the Dalian Institute of Chemical Physics of the Chinese Academy of Sciences identified the key glycosyltransferase that catalyzes the conversion of Reb D to Reb M, and revealed the molecular mechanism underlying its substrate regioselectivity.

Researchers first identified and characterized UGT76G4, a natural variant of UGT76G1, from a high-Reb M producing Stevia cultivar. They discovered that UGT76G4 exhibited regioselectivity toward the C19 position of steviol glycosides in both in vivo and in vitro assays, thereby confirming it as the key enzyme catalyzing the conversion of Reb D to Reb M.

Then, researchers systematically elucidated the molecular basis of UGT76G4 regioselectivity, and identified residue G200 as critical for its C19 catalytic activity.

Furthermore, researchers engineered several tool enzymes with enhanced performance by applying semi-rational design. They engineered UGT76G4 variants capable of efficiently synthesizing Reb M using Rebaudioside E (Reb E) and Reb D as substrates.

“This work not only clarifies the question of which enzyme is responsible for Reb M biosynthesis, but also provides engineered biocatalysts to enable the efficient production of this next generation natural sweetener,” said Prof. Yin.

Farmers are under pressure. Fertilizer costs have soared in recent years. Tariffs are increasing equipment costs and cutting Canadian farmers off from key foreign markets. And climate change is bringing its own set of challenges.

Meanwhile, agriculture is also facing calls to reduce emissions. The industry is responsible for about 10% of Canada’s greenhouse gas emissions, and the federal government has set an ambitious goal: reduce emissions from fertilizer use by 30% by 2030.

Farming is tough even during the best of times. Rising costs and the dangers posed by climate change will only make it even more challenging in the years to come.

That’s where our work comes in. At MacEwan University, through our spin-out company PimaSens, we have developed Agrilo—a low-cost soil testing sensor paired with a smartphone app.

Our goal is simple: give farmers clear, real-time guidance on fertilizer use so they can save money, boost yields and protect the environment.

How the sensor works

Agrilo takes technology we first built in the lab and translates it into an easy-to-use diagnostic tool for the field. Unlike traditional soil testing, which often requires sending samples to a lab and waiting days for results, Agrilo provides answers in minutes.

xFarmers can select the tests most relevant to their crops and soils. These results feed directly into Agrilo’s smartphone app, which analyzes patterns and suggests the most optimal fertilizer adjustments.

Each Agrilo sensor costs about $10 and is designed to detect a specific nutrient or soil property. The full suite includes sensors for: nitrate, phosphate, potassium, pH, sulfur, magnesium, manganese, calcium, boron, iron, natural organic matter, cation exchange capacity and more.

Farmers can select the tests most relevant to their crops and soils. These results feed directly into Agrilo’s smartphone app, which analyzes patterns and suggests the most optimal fertilizer adjustments.

This precision is critical. Overuse of fertilizer wastes money and increases greenhouse gases, while underuse limits yields. Getting the balance right improves farm efficiency and protects ecosystems.

With fertilizer shortages, soil degradation accelerating and climate concerns mounting, there is an urgent need for practical solutions that can be deployed quickly and affordably.

For farmers, the value is clear:

Healthier soil through balanced nutrient application.

Higher crop yields from optimized fertilizer use.

Lower costs by reducing waste.

Reduced environmental harm from nutrient runoff and fertilizer-related emissions.

The research behind the tool

Our sensors and platform have been validated in peer-reviewed research with the Agrilo version simplified for ease of use by farmers. We also hold a provisional patent, with a full filing in progress. This ensures that the innovation is both scientifically sound and protected for scaling.

Agrilo was created to be both affordable and accessible. Conventional soil testing often costs hundreds of dollars and involves long wait times. Agrilo delivers the same type of data—validated against results from traditional labs—at a fraction of the cost and in real time.

This opens up opportunities not just for Canadian farmers but also for communities worldwide, including schools and small scale farmers in the Global South.

One of the most exciting aspects of Agrilo is its versatility. Beyond the farm, Agrilo doubles as an education platform. In classrooms, students can learn hands-on how soil nutrients affect crops, food security and ecosystems.

Using the same colorimetric sensors as farmers, students can connect textbook science to real-world environmental challenges—making soil chemistry, agriculture and sustainability more tangible.

Globally, fertilizer use has increased by 46% since 1990. About one third of the world’s soils are already degraded, with degradation continuing to accelerate.

By making precision agriculture practical and affordable, we can help address these challenges at scale—showcasing how research developed in Canadian labs can benefit farms, classrooms and communities worldwide.

Looking ahead

Our team is continuing to refine Agrilo. We are already testing the platform with farmers and partners in Canada, Kenya, Costa Rica and beyond.

At the same time, we are building partnerships with schools and international organizations to use Agrilo as both a farming tool and a hands-on educational resource. Several high schools in Alberta have started to try out the Agrilo tool to enhance applied science learning.

Ultimately, our vision is to make precision agriculture accessible to everyone—not just large-scale industrial operations. With the right tools, all farmers can play a critical role in feeding the world sustainably, protecting ecosystems and helping their countries meet their climate goals.