Amino acid and peptide derivatives of dimethyl 5-aminoisophthalate as fluorogenic substrates for proteinases |
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Authors: | N. Baggett N. Blake J. Boukouvalas A.K. Samra C.J. Gray |
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Affiliation: | Department of Chemistry, University of Birmingham, P.O. Box 363, Birmingham B15 2TT, UK |
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Abstract: | A number of amino acid and peptide derivatives of the fluorophore, dimethyl 5-aminoisophthalate have been synthesized, characterized and tested as substrates for the plant cysteine proteinases papain, ficin and bromelain. In every case, replacement of alanine by citrulline, in the position adjacent to the dimethyl 5-aminoisophthalate resulted in a higher rate of hydrolysis. The partly deprotected dipeptide derivative dimethyl phenylalanylcitrulline-5-aminoisophthalate was hydrolysed most rapidly of all the compounds tested, and on this basis may provide a useful substrate for the detection and quantitative assay of these enzymes. |
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Keywords: | Enzyme enzyme assays dimethyl 4-aminoisophthalate fluorogenic substrates proteinases |
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