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"Cancer cells undergo complex metabolic changes and require the amino acid L-asparagine (ASN) to grow. Starving cancers by depriving them of ASN is a powerful anticancer strategy, notably in the treatment of Acute Lymphoblastic Leukaemia (ALL). ALL is the most common cancer in children, however adults with the disease have a particularly poor survival outlook and represent a disproportionately high public health burden. A cornerstone therapy in the treatment of ASN-avid cancers like ALL is the enzyme L-asparaginase (ASNase), which converts ASN into aspartate which the cancer cells cannot use, thus starving them. Current ASNase drugs use enzymes derived from bacteria, which can invoke allergic reactions in patients, and they do not last very long in the bloodstream, increasing the frequency of treatments. Newer versions of the drug are modified to improve on these issues, but they still suffer from liver toxicity arising from side-effects relating to the glutaminase (GLS; metabolism of glutamine) activity of the ASNase. As a result, there is a significant proportion of patients who have very low tolerability for ASNase treatment and therefore an unmet clinical need for a fully human-compatible ASNase with minimal side-effects. The **humaNase** project aims to address these needs by characterising a safer, human-derived ASNase alternative. We recently discovered a type of GLS-free ASNase called human Asparaginase-like protein 1 (hASRGL1) in vesicles secreted by human stem cells; our goal is to compare and contrast the efficacy of this enzyme to currently employed _bacterial_ ASNases, with an eye towards the eventual adoption of hASRGL1 as a more tolerable chemotherapeutic. Towards that end, we aim to perform a series of assays to quantify the activity, stability, safety, and cancer cell-killing ability of the human-derived enzyme. This preliminary characterisation of the therapeutically-relevant properties of hASRGL1, using current bacterial ASNases as a benchmark, is a fundamental first step in establishing the feasibility of employing the enzyme as a potentially safer and more tolerable alternative to current ALL treatments. Moreover, the results of the project are intended to drive the development of a more elaborate drug-delivery platform, based on the hASRGL1 enzyme, for broader and more efficacious chemotherapeutic applications."

Picture a band-aid. Visualise how thin, flexible and light it is. How it adapts its shape to your body and how reassuring and seamless it feels to have it on. Now imagine that band-aid is a personal well-being monitor with sensors measuring health and environmental parameters and the capacity to communicate wirelessly with the wearer and the carer when a potential risk situation is detected. Technology development in energy systems and sensing electronics is finally at a point where the development of the product described can be made a reality. Enter: RE-Patch. This project is focused on developing a low-cost smart wearable biomedical patch powered by an ultra-thin and flexible energy source. Two UK companies have partnered to achieve this by miniaturising an existing biomedical patch- developed and patented by one of the partnering companies- and integrating an energy system that includes a thin and flexible battery and a supercapacitor –developed and patented by the second partner.