ArticleScientific reports2022
Characterization and molecular docking study of cathepsin L inhibitory peptides (SnuCalCpIs) from Calotropis procera R. Br.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Cysteine Peptidases ofCurrent protein & peptide science · 2025Review
- Cysteine protease I29 propeptide from Calotropis procera R. Br. As a potent cathepsin L inhibitor and its suppressive activity in breast cancer metastasis.Scientific reports · 2024Article
- Identification of Z-Tyr-Ala-CHNMicroorganisms · 2023Article
- In-silico investigation of a novel inhibitors against the antibiotic-resistantSaudi journal of biological sciences · 2022Article
- Aspartate α-decarboxylase a new therapeutic target in the fight againstFrontiers in microbiology · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Propeptides, released from the autocatalytic activation of its zymogen, are potential inhibitors against proteases involved in cancer cell invasion and migration. Our research team previously obtained novel propeptides (SnuCalCpIs) from transcriptome analysis of the medicinal plant Calotropis procera R. Br. and reported them as promising candidates for cancer therapeutics due to their cathepsin L inhibition activity. In the present study, inhibitory activity among SnuCalCpIs was compared with inhibition efficiency and verified by in silico molecular docking analysis. Only SnuCalCpI03 and SnuCalCpI15, expressed in Escherichia coli, showed inhibitory activity against cathepsin L as competitive inhibitors, and the half-maximal inhibitory concentrations (IC
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