Therapeutic Protease and Peptidase Inhibitors

Dear Colleagues,

The human genome encodes 600–700 proteases (2–3% of genes), defined as hydrolytic enzymes that break down proteins. Digestive proteases were initially characterized, but it was soon understood that proteases mediate many physiological functions in both intra- and extracellular compartments. Protein turnover, autophagy, hormonal maturation and degradation, tissue homeostasis, blood coagulation, cell proliferation, and viral infections are a few examples illustrating the importance of proteases.  Peptidases, which hydrolyze smaller substrates such as peptide hormones, are also of prime physiological importance. Proteases and peptidases belong to diverse families according to their catalytic mechanisms (serine proteases, metalloproteinases/peptidases, cysteine, and aspartic proteases).

Therapeutic inhibitors of proteases and peptidases have increasing importance as drugs, either in the form of small molecules (e.g., angiotensin-converting enzyme inhibitors) or proteins of high specificity. Biologic protease inhibitors exploited in therapeutics include replacement therapy of a deficient or dysfunctional protein (e.g., C1 esterase inhibitor) and engineered inhibitory proteins such as monoclonal antibodies, darpins, and Kunitz domain derivatives. Drugs and Drug Candidates invites submissions for this Special Issue titled "Therapeutic Protease and Peptidase Inhibitors".

Dr. François Marceau
Guest Editor

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• protease inhibitors
• peptidase inhibitors
• small molecule protease inhibitors
• engineered protein inhibitors
• proteases
• peptidases