Polypeptides. Part XIV. A comparative study of the stability towards enzymes of model tripeptides containing α-aza-amino-acids,L-amino-acids, andD-amino-acids
- 1 January 1976
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Perkin Transactions 1
- No. 2,p. 244-248
- https://doi.org/10.1039/p19760000244
Abstract
The stability of three model tripeptides, L-lysyl-α-aza-phenylalanyl-L-leucine, L-lysyl-L-phenylalanyl-L-leucine, and L-lysyl-D-phenylalanyl-L-leucine, towards aminopeptidase, carboxypeptidase, thermolysin, and trypsin has been investigated. These tripeptides were synthesised by the classical method of peptide synthesis. The α-aza-phenylalanine-containing tripeptide was stable to the first three of these enzymes, but the L-lysyl–α-aza-phenylalanine bond was readily cleaved by trypsin. The tripeptide containing D-phenylalanine was stable to all these enzymes, whereas the tripeptide with L-phenylalanine was completely cleaved in 72 h.Keywords
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