A class of enzymes known as proteases is responsible for catalyzing the breakdown of covalent peptide bonds. Proteases account for almost 2% of the genes in humans, infectious organisms, and other forms of life. Serine proteases, so named because they have a nucleophilic serine residue at the active site, make for nearly one-third of all proteases. Although digesting is their primary role in humans, they also play roles in immunological response, apoptosis, inflammation, blood coagulation, and signal transduction. They are therefore very attractive biological targets for the design of pharmacological molecules that can modulate their activity. This review presents a description of the catalytic activity and structure of serine proteases, and the different strategies to develop inhibitors. Serine protease inhibitors targeting thrombin, FXa, and human neutrophil elastase (HNE), and dipeptidylprotease-4 (DPP4) will be described. It includes therapeutically applied, and those drugs which are still under investigation in clinical trials in the last two decades.
Ramadan, M. (2023). REVIEW OF SERINE PROTEASE INHIBITORS: DEVELOPMENT AND APPLICATIONS. Bulletin of Pharmaceutical Sciences Assiut University, 46(2), 835-854. doi: 10.21608/bfsa.2023.327340
MLA
Mai Abed ElRahman Ramadan. "REVIEW OF SERINE PROTEASE INHIBITORS: DEVELOPMENT AND APPLICATIONS". Bulletin of Pharmaceutical Sciences Assiut University, 46, 2, 2023, 835-854. doi: 10.21608/bfsa.2023.327340
HARVARD
Ramadan, M. (2023). 'REVIEW OF SERINE PROTEASE INHIBITORS: DEVELOPMENT AND APPLICATIONS', Bulletin of Pharmaceutical Sciences Assiut University, 46(2), pp. 835-854. doi: 10.21608/bfsa.2023.327340
VANCOUVER
Ramadan, M. REVIEW OF SERINE PROTEASE INHIBITORS: DEVELOPMENT AND APPLICATIONS. Bulletin of Pharmaceutical Sciences Assiut University, 2023; 46(2): 835-854. doi: 10.21608/bfsa.2023.327340
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