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Reactivity of Lys(NH 2 )‐containing peptides toward endopeptidases
Author(s) -
Samson Fabrice,
Bonnet Dominique,
Rommens Corinne,
GrasMasse Hélène,
Melnyk Oleg
Publication year - 1999
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199908)5:8<352::aid-psc207>3.0.co;2-o
Subject(s) - reactivity (psychology) , chemistry , stereochemistry , biochemistry , combinatorial chemistry , medicine , pathology , alternative medicine
Lys(NH 2 )‐containing peptides were subjected to various proteolytic enzymes which were selected for their well‐documented specificity for arginyl and/or lysyl peptide bonds. Lys(NH 2 )‐containing peptides were cleaved more rapidly by clostripain than the corresponding lysyl peptides. On the other hand, they proved to be resistant to Achromobacter protease I hydrolysis. The modified peptides synthesized in this study were more stable than the arginyl and lysyl analogues when incubated with trypsin or thrombin. The same tendency was observed when Lys(NH 2 )‐containing peptides were incubated in diluted human serum, suggesting that the replacement of Arg or Lys by Lys(NH 2 ) could be used to increase the stability of peptides in vivo . Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.