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Researchers chart new course for AI-powered biomedical discoveries

University of Missouri researchers are paving the way as artificial intelligence transforms biomedical research. A team from the College of Engineering and collaborators recently published one of the most comprehensive reviews to date of an emerging AI approach for biology known as flow matching. The work, published in Nature Machine Intelligence, provides scientists around the world with a roadmap for applying the technology to accelerate drug discovery, precision medicine and other biomedical advances.

“Flow matching helps computers learn how biology changes from one state to another,” said Jianlin “Jack” Cheng, a Curators’ Distinguished Professor and Paul K. and Diane Shumaker Professor in Bioinformatics. “This gives scientists a powerful new way to study everything from protein folding to cell development and cancer progression.”

AI reveals new class of cellular ‘off switch’ linked to cancer pathways

Cornell researchers have used artificial intelligence to uncover a previously unknown way cells control how proteins move inside them, a process essential for growth, communication and movement, and one that is often disrupted in cancer.

The study, published Sept.9 in the Journal of Cell Biology, shows that a little-understood protein called Avl9 acts as an “off switch” for another protein, Arf1, which helps direct where materials go inside cells. Turning Arf1 off at the right time is critical as it regulates cellular transport, otherwise cells become disorganized which leads to negative effects. The researchers also found that Avl9 is part of a broader group of proteins that may perform the same function, pointing to a previously unrecognized system cells use to keep this process in balance.

Led by Chris Fromme, professor of molecular biology and genetics at the College of Agriculture and Life Sciences and faculty in the Weill Institute for Cell and Molecular Biology, the team used AlphaFold, an artificial intelligence software that predicts the structures of proteins and how they might interact, to search for previously unknown partners of Arf1.

Google DeepMind publishes AIpowered predictions for the effect of all 9 billion possible singlepoint mutations to human DNA

DeepMind’s catalogue of predicted DNA mutation effects, could help scientists unlock the cause of rare genetic diseases and help them find cures.

Scientists engineer ready-to-use cancer-fighting T cells for solid tumors

T-cell receptor, or TCR, therapy is a cancer treatment that genetically reprograms immune cells, called T cells, to hunt down cancer with precision. It’s similar to another treatment, CAR T-cell therapy, but with one key difference: CAR T-cell therapy can only spot proteins that naturally appear outside a cancer cell. TCR therapy, however, can also catch small protein fragments from inside the cell that are carried to the surface and displayed like little name tags.

Tiny molecular rings open new ways for designing better medicines

Cyclopropanes are organic chemistry’s smallest rings. Three carbon atoms are joined in a triangle, creating a compact and unusually strained structure. Despite—or partly because of—this unusual geometry, cyclopropanes are found in many biologically active natural products and have important applications in medicines and drug discovery, from antidepressants to antibiotics and antiviral research.

Connect these carbon triangles to an amine, a functional group with a nitrogen at its center, and you get aminocyclopropanes. They are of particular interest in pharmaceutical research because they can be used to replace another substructure commonly found in drug molecules: α,α-gem-dimethylamines (compounds in which the aminocyclopropane’s triangle is “opened” by disconnecting one edge).

Such molecular substitutes that resemble an existing part of a drug but can alter important properties, such as biological activity and metabolic stability, are referred to as bioisosteres and have shown beneficial effects in countless cases.

Untangling the meta-biomaterial puzzle one property at a time

From repairing damaged tissues to developing better implants, many medical developments depend on materials that can mimic the complex properties of human tissue. Meta-biomaterials are among the most promising candidates. By tailoring their geometry, researchers can create materials with properties similar to those of natural tissues. But there is a catch: Changing one property often changes several others at the same time. TU Delft scientists have now developed a method to decouple these properties.

Their work, published in Nature Communications, helps researchers understand how individual material properties influence cell behavior and could accelerate the development of next-generation biomaterials.

Meta-biomaterials are engineered materials whose properties are determined not by their chemical composition but by their internal architecture. This allows researchers to design structures with carefully tuned mechanical, morphological and mass-transport properties. Such control is particularly valuable in biomedical engineering, where materials need to do more than simply replace damaged tissue. They must also interact with cells and actively support tissue regeneration.

Depression in Later Life May Be an Early Warning Sign of Alzheimer’s

Depression in later life may be an early warning from the brain, appearing years before Alzheimer’s begins to affect memory and thinking

A new study in JNeurosci found that faster accumulation of tau, a protein closely tied to Alzheimer’s, was associated with worsening depressive symptoms in older adults who remained cognitively healthy. Teodora Markova of Brandeis University and her colleagues investigated whether changes in mood might track the gradual buildup of tau in the aging brain.

Tau normally helps support the internal structure of neurons. When it becomes abnormal, however, it can collect into tangles that interfere with brain function. These tangles are one of the defining biological features of Alzheimer’s disease, alongside deposits of amyloid beta.

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