Lancaster University

Biochemists aim to reengineer photosynthesis to address a looming food crisis due to global warming and population growth. The process, particularly the enzyme RuBisCO, is inefficient, often grabbing oxygen instead of CO2. The RIPE Project, funded by the Gates Foundation, seeks to improve photosynthesis efficiency, potentially doubling food output by tweaking RuBisCO and other aspects of the process. Challenges include balancing thousands of chemical reactions and convincing the public of the benefits of genetically modified crops.

Researchers from Lancaster University developed RI-AG03, a peptide inhibitor preventing Tau protein build-up in Alzheimer's disease. RI-AG03 targets both aggregation-promoting areas of Tau, potentially leading to more effective treatments. Lab studies and tests on genetically modified fruit flies showed significant suppression of neurodegeneration and extended lifespan. Human cell line tests also indicated reduced Tau fibril formation. The dual-targeting mechanism of RI-AG03 could offer safer treatment options compared to current therapies. Further research in rodents and clinical trials in humans are planned.

RI-AG03, a new peptide inhibitor, effectively targets both major aggregation-promoting hotspots of Tau proteins in lab and fruit fly studies, potentially improving Alzheimer’s treatment safety and efficacy.

A new drug, RI-AG03, targets two key regions of the tau protein, preventing its toxic build-up and showing promise in treating Alzheimer’s disease, as demonstrated in lab and fruit fly studies. Further research, including clinical trials, is necessary to validate its efficacy in humans.

Scientists developed RI-AG03, a peptide inhibitor targeting both major Tau protein hotspots, effective in preventing Tau build-up in lab and fruit fly studies. Dr. Aggidis, former Postdoctoral Research Associate at Lancaster University, believes this could lead to treatments for Alzheimer’s disease. The research, published in Alzheimer’s & Dementia, was a collaborative effort involving multiple institutions.

RI-AG03, a peptide inhibitor, effectively prevents Tau protein accumulation in Alzheimer's disease, targeting both key regions of the protein. Tested in fruit flies and biosensor cells, it extended life and reduced aggregation, with plans for rodent trials before clinical testing.

Scientists developed a drug, RI-AG03, targeting tau proteins to combat Alzheimer’s, showing efficacy in lab and fruit fly studies. The drug inhibits key regions affected by the disease, potentially offering more effective treatment with fewer side effects.

A new Alzheimer’s drug, RI-AG03, targets both key areas of tau proteins, preventing their build-up in lab and fruit fly studies, potentially leading to more effective treatments.

Scientists developed RI-AG03, a novel Alzheimer's drug targeting tau protein aggregation at two key sites, showing promise in cell and fruit fly studies. Collaboration among multiple institutions led to this breakthrough, potentially paving the way for more effective treatments.

Researchers developed RI-AG03, a peptide inhibitor targeting Tau protein aggregation hotspots, showing efficacy in preventing aggregation and extending lifespan in fruit fly models, with potential for Alzheimer’s treatment.