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Scientists propose new strategies to find drugs that neutralize critical enzymes

Scientists propose new strategies to find drugs that neutralize critical enzymes May 26 2021 Scientists from the University of Bath explore racemases and propose strategies for finding drugs that target these important enzymes. The active site of alanine racemase, a key antibacterial target. Image Credit: University of Bath Academics from the University of Bath explore racemases – an important type of enzyme that is linked to certain cancers and other life-threatening diseases while also being critical to cell function – in a paper published in the prestigious journal Chemical Society Reviews. The scientists also propose new strategies for finding drugs that neutralize these enzymes.

Racemases: The hunt for drugs to neutralise these critical enzymes

Credit: University of Bath Scientists from the UK s University of Bath explore racemases - an important type of enzyme that is linked to certain cancers and other life-threatening diseases while also being critical to cell function - in a paper published in the prestigious journal Chemical Society Reviews. The scientists also propose new strategies for finding drugs that neutralise these enzymes. Many racemases and epimerases perform vital roles in human and animal cells, and in disease-causing organisms. They facilitate proper nerve function, the degradation of toxic substances, the formation of bacterial cell walls and the conversion of certain drugs into their active form (the best known conversion is seen with ibuprofen, which is taken as a mixture of isomers and converted in the liver to the active S-isomer). But while normal levels of racemase and epimerase function are generally beneficial, increased levels can be harmful. Because of this, there is considerable interest in

Understanding the growth of disease-causing protein fibres

 E-Mail IMAGE: Transmission Electron Micrograph of fibrils from the protein alpha-synuclein, which is associated with Parkinson s disease. view more  Credit: University of Bath Amyloid fibrils are deposits of proteins in the body that join together to form microscopic fibres. Their formation has been linked to many serious human diseases including Alzheimer s, Parkinson s and Type 2 diabetes. Until today, scientists have been unable to reliably measure the speed of fibril growth, as there have been no tools that could directly measure growth rate in solution. However, researchers from the UK s University of Bath and the ISIS Neutron and Muon Source have now invented a technique that does just that. Results from their study are published in

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