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Design of selective substrates of proteinase 3 using combinatorial chemistry methods
- Source :
-
Analytical Biochemistry . Jul2008, Vol. 378 Issue 2, p208-215. 8p. - Publication Year :
- 2008
-
Abstract
- Abstract: In this study, chemical synthesis of the selective chromogenic/fluorogenic substrates for proteinase 3 is described. The substrates’ sequence was obtained using combinatorial chemistry methods. Deconvolution of the tripeptide library against proteinase 3 with general formula ABZ-X3-X2-X1-ANB-NH2 yielded the active sequence. Selected peptide was further modified on its C terminus to investigate the impact of chromophore moiety modification on enzyme–substrate interaction. To determine specificity, activity of selected substrates was characterized against proteinase 3 and neutrophil elastase. Finally, the peptide ABZ-Tyr-Tyr-Abu-ANB-NH2 displayed the highest value of specificity constant (k cat/K M =189×103 M−1 s−1) for proteinase 3. To the best of our knowledge, this is the first short peptide that undergoes selective proteolysis by proteinase 3 and displays no significant hydrolysis in the presence of human neutrophil elastase and cathepsin G. [Copyright &y& Elsevier]
- Subjects :
- *PROTEOLYTIC enzymes
*PEPTIDASE
*PROTEINASES
*AMINOPEPTIDASES
Subjects
Details
- Language :
- English
- ISSN :
- 00032697
- Volume :
- 378
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Analytical Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 32560605
- Full Text :
- https://doi.org/10.1016/j.ab.2008.04.003