Neffe, A.Abell, A.2007-07-052007-07-052005Current Opinion in Drug Discovery and Development, 2005; 8(6):684-7001367-67332040-3437http://hdl.handle.net/2440/34465Calpains are Ca(2+)-dependent cysteine proteases that play an important role in cell differentiation and in apoptosis/necrosis. The overactivation of calpain is connected with a number of diseases, including cataracts and traumatic brain injury, making calpain an attractive drug target. The development of selective inhibitors of calpain has, however, proved difficult, due to a lack of detailed structural information on the protein. This difficulty has been somewhat alleviated with recent reports on the X-ray crystal structures of engineered calpains and improved biochemical characterization of the protein. This review describes properties and X-ray crystal structures of calpain, and the synthesis and binding affinities of novel calpain inhibitors.enAldehydesAmidesBiphenyl CompoundsCalpainPeptidesProdrugsCysteine Proteinase InhibitorsCrystallography, X-RayInhibitory Concentration 50Binding SitesProtein ConformationDrug DesignSolubilityJournal article00200644540002333317000022-s2.0-2784446203650296Abell, A. [0000-0002-0604-2629]