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Synthesis of Tetrapeptide p-nitrophenylanilides containing dehydroalanine and dehydrophenylalanine and their influence on cathepsin C activity
Three dehydrotetrapeptides of rationally varying structure were prepared and tested as affectors of cathepsin C. These compounds appeared to be substrates of the enzyme, being equipotent with their classical counterparts. Thus, replacement of amino acid in a short peptide by corresponding dehydroami...
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| Published in: | Journal of peptide science 2001-03, Vol.7 (3), p.141-145 |
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| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c3827-2f509ef18e7bb4d3fbd3d5e02d46f01fc9252cbb9809ac32848a4d7866c8a7183 |
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| cites | cdi_FETCH-LOGICAL-c3827-2f509ef18e7bb4d3fbd3d5e02d46f01fc9252cbb9809ac32848a4d7866c8a7183 |
| container_end_page | 145 |
| container_issue | 3 |
| container_start_page | 141 |
| container_title | Journal of peptide science |
| container_volume | 7 |
| creator | Makowski, Maciej Pawełczak, Małgorzata Latajka, Rafał Nowak, Kornel Kafarski, Paweł |
| description | Three dehydrotetrapeptides of rationally varying structure were prepared and tested as affectors of cathepsin C. These compounds appeared to be substrates of the enzyme, being equipotent with their classical counterparts. Thus, replacement of amino acid in a short peptide by corresponding dehydroamino acid does not prevent cathepsin C in recognizing dehydropeptide as its substrate. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd. |
| doi_str_mv | 10.1002/psc.307 |
| format | article |
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These compounds appeared to be substrates of the enzyme, being equipotent with their classical counterparts. Thus, replacement of amino acid in a short peptide by corresponding dehydroamino acid does not prevent cathepsin C in recognizing dehydropeptide as its substrate. 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Peptide Sci</addtitle><description>Three dehydrotetrapeptides of rationally varying structure were prepared and tested as affectors of cathepsin C. These compounds appeared to be substrates of the enzyme, being equipotent with their classical counterparts. Thus, replacement of amino acid in a short peptide by corresponding dehydroamino acid does not prevent cathepsin C in recognizing dehydropeptide as its substrate. 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| fulltext | fulltext |
| identifier | ISSN: 1075-2617 |
| ispartof | Journal of peptide science, 2001-03, Vol.7 (3), p.141-145 |
| issn | 1075-2617 1099-1387 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77032979 |
| source | Wiley-Blackwell Read & Publish Collection |
| subjects | Alanine - analogs & derivatives Alanine - chemistry Amino Acids - chemistry Anilides - chemical synthesis Anilides - chemistry Animals Cathepsin C - chemistry Cathepsin C - metabolism Cattle dehydroamino acids dipeptidyl-peptidase I Magnetic Resonance Spectroscopy Models, Chemical Oligopeptides - chemical synthesis Oligopeptides - chemistry Phenylalanine - analogs & derivatives Phenylalanine - chemistry proteolytic enzymes Spleen - metabolism |
| title | Synthesis of Tetrapeptide p-nitrophenylanilides containing dehydroalanine and dehydrophenylalanine and their influence on cathepsin C activity |
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