Synthesis and Biological Activity of N-Sulfonyltripeptides with C-Terminal Arginine as Potential Serine Proteases Inhibitors
| Autor: | Arkadiusz Surażyński, Magdalena Bruzgo, Ewa Gorodkiewicz, Agnieszka Markowska |
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| Rok vydání: | 2012 |
| Předmět: |
Serine proteases inhibitor
Urokinase Surface Plasmon Resonance Imaging Chemistry Plasmin Bioengineering Tripeptide Kallikrein Trypsin Biochemistry Article Analytical Chemistry Serine chemistry.chemical_compound Thrombin Drug Discovery Cancer cells activity medicine Amidolytic activity Molecular Medicine Urokinase inhibitor Norvaline medicine.drug |
| Zdroj: | International Journal of Peptide Research and Therapeutics |
| ISSN: | 1573-3904 1573-3149 |
| DOI: | 10.1007/s10989-012-9338-4 |
| Popis: | Tripeptides of the general X-SO2-d-Ser-AA-Arg-CO-Y formula, where X = α-tolyl, p-tolyl, 2,4,6-triisopropylphenyl; AA = alanine, glycine, norvaline and Y = OH, NH-(CH2)5NH2 were obtained and tested for their effect on the amidolytic activities of urokinase, thrombin, trypsin, plasmin, t-PA and kallikrein. The most active compound towards urokinase was PhCH2SO2-d-Ser-Gly-Arg-OH with Ki value 5.4 μM and the most active compound toward thrombin was PhCH2SO2-d-Ser-NVa-Arg-OH with Ki value 0.82 μM. The peptides were nontoxic against porcine erythrocytes in vitro. PhCH2SO2-d-Ser-Gly-Arg-OH showed cytotoxic effect against DLD cell lines with IC50 values of 5 μM. For the highly selective determination of the interaction of some of the synthesised acids of tripeptides with urokinase and plasmin the Surface Plasmon Resonance Imaging sensor has been applied. These compounds bind to urokinase and plasmin in 0.05 mM concentration. |
| Databáze: | OpenAIRE |
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