Cysteine Proteases Inhibitors Library
Cysteine Protease Inhibitors Library
ChemDiv’s library of cysteine protease inhibitors contains 7,801 compounds.
Cysteine proteases are a class of enzymes that are involved in various physiological processes, including protein degradation and processing. Their malfunction or dysregulation can contribute to the pathogenesis of multiple diseases. Apart from cysteine proteases, there are three main classes of protease enzymes, namely, serine proteases, aspartic proteases, and metalloproteases. Normally, Cysteine proteases belonging to the papain family enzymes, are involved in multiple functions such as extracellular matrix turnover, antigen presentation, processing events, digestion, immune invasion, hemoglobin hydrolysis, parasite invasion, parasite egress, and processing surface proteins [1]. In cancer, abnormal activity of cysteine proteases can lead to tumor progression and metastasis by degrading extracellular matrix components and modulating cell signaling pathways. In neurodegenerative disorders such as Alzheimer's disease, aberrant activity of those enzymes is related to the formation of amyloid plaques and neurofibrillary tangles that are known as main factors contributing to neuronal damage and disease progression. Additionally, in infectious diseases, certain pathogens utilize cysteine proteases to evade the host's immune response or to process their own proteins, making these enzymes potential targets for therapeutic intervention. Therefore, modulating cysteine protease activity holds significant potential in the development of treatments for a variety of diseases, including cancer, neurodegenerative disorders, and infections.
Protease inhibitors have wide-ranging applications in both medicine and biotechnology fields. These inhibitors are implemented in the treatment of cancer, hypertension, thrombosis, diabetes, and viral and bacterial infections. They often function by mimicking the peptide substrates of their target enzymes and possess specialized structural components that interact specifically with the catalytic residues in the enzyme's active site. When targeting cysteine proteases, traditional inhibitors typically utilize activated electrophiles, such as epoxides or vinyl sulfones, to engage with the enzyme. This interaction often leads to the inhibition of the protease's enzymatic activity, thereby modulating the biological pathways in which these enzymes are involved. The precise interaction between cysteine protease inhibitors and their target proteases is critical for developing effective therapeutic agents for abovementioned diseases [2].
References
[1] S. Verma, R. Dixit, and K. C. Pandey, “Cysteine proteases: Modes of activation and future prospects as pharmacological targets,” Front. Pharmacol., vol. 7, no. APR, pp. 1–12, 2016, doi: 10.3389/fphar.2016.00107.
[2] L. Kaysser, “Built to bind: Biosynthetic strategies for the formation of small-molecule protease inhibitors,” Nat. Prod. Rep., vol. 36, no. 12, pp. 1654–1686, 2019, doi: 10.1039/c8np00095f.
ChemDiv’s library of cysteine protease inhibitors contains 7,801 compounds.
Cysteine proteases are a class of enzymes that are involved in various physiological processes, including protein degradation and processing. Their malfunction or dysregulation can contribute to the pathogenesis of multiple diseases. Apart from cysteine proteases, there are three main classes of protease enzymes, namely, serine proteases, aspartic proteases, and metalloproteases. Normally, Cysteine proteases belonging to the papain family enzymes, are involved in multiple functions such as extracellular matrix turnover, antigen presentation, processing events, digestion, immune invasion, hemoglobin hydrolysis, parasite invasion, parasite egress, and processing surface proteins [1]. In cancer, abnormal activity of cysteine proteases can lead to tumor progression and metastasis by degrading extracellular matrix components and modulating cell signaling pathways. In neurodegenerative disorders such as Alzheimer's disease, aberrant activity of those enzymes is related to the formation of amyloid plaques and neurofibrillary tangles that are known as main factors contributing to neuronal damage and disease progression. Additionally, in infectious diseases, certain pathogens utilize cysteine proteases to evade the host's immune response or to process their own proteins, making these enzymes potential targets for therapeutic intervention. Therefore, modulating cysteine protease activity holds significant potential in the development of treatments for a variety of diseases, including cancer, neurodegenerative disorders, and infections.
Protease inhibitors have wide-ranging applications in both medicine and biotechnology fields. These inhibitors are implemented in the treatment of cancer, hypertension, thrombosis, diabetes, and viral and bacterial infections. They often function by mimicking the peptide substrates of their target enzymes and possess specialized structural components that interact specifically with the catalytic residues in the enzyme's active site. When targeting cysteine proteases, traditional inhibitors typically utilize activated electrophiles, such as epoxides or vinyl sulfones, to engage with the enzyme. This interaction often leads to the inhibition of the protease's enzymatic activity, thereby modulating the biological pathways in which these enzymes are involved. The precise interaction between cysteine protease inhibitors and their target proteases is critical for developing effective therapeutic agents for abovementioned diseases [2].
References
[1] S. Verma, R. Dixit, and K. C. Pandey, “Cysteine proteases: Modes of activation and future prospects as pharmacological targets,” Front. Pharmacol., vol. 7, no. APR, pp. 1–12, 2016, doi: 10.3389/fphar.2016.00107.
[2] L. Kaysser, “Built to bind: Biosynthetic strategies for the formation of small-molecule protease inhibitors,” Nat. Prod. Rep., vol. 36, no. 12, pp. 1654–1686, 2019, doi: 10.1039/c8np00095f.