Abstract
In most organisms around 2% of the genes code for peptidases being this number only surmounted by the genes that code for transcriptional factors. This ubiquitous presence is almost unequaled and has for long fascinated biochemists. Although peptidases have been classified in four mechanistic classes (aspartic-, cysteine-, serine- and metallo-peptidases), the more recent MEROPS database recognizes 42 evolutionary distinct peptidase structures corresponding to 42 different families. As peptidases are involved in several physiological processes they are an obvious target for the development of therapeutic agents to treat infectious disease. The Trypanosomatidae family includes etiologic agents for human and veterinary diseases, such as Trypanosoma cruzi, Leishmania spp. and the African trypanosomes that are responsible for the Chagas disease, for a wide spectrum of clinical manifestations known as leishmaniasis, and for the “sleeping sickness”, respectively. These microorganisms present a complex life cycle that includes dimorphic developmental stages in distinct hosts and by extension show nutritional adaptation. This review covers the recent advances in the biochemical characterization of trypanosomatid proteolytic enzymes and that of specific inhibitors to block their hydrolytic activity, in accordance to the peptidases potential role as target to the treatment of the aforementioned illnesses.
Keywords: Trypanosomatidae family, Trypanosoma, Leishmania, chagas disease, eishmaniasis, sleeping sickness, trypanosomatidae peptidases, peptidases, proteolysis, peptidases inhibitors
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