Reactivity of Lys(NH2)-containing peptides toward endopeptidases

• Published in: Journal of peptide science Vol. 5; no. 8; pp. 352 - 359
• Main Authors: Samson, Fabrice, Bonnet, Dominique, Rommens, Corinne, Gras-Masse, Hélène, Melnyk, Oleg
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.08.1999
• Subjects: Achromobacter; Achromobacter protease I; Alcaligenes - enzymology; Amino Acid Sequence; clostripain; Endopeptidases - metabolism; Humans; Hydrolysis; Lys(NH2)-containing peptides; Lysine - metabolism; Peptides - blood; Peptides - chemistry; Peptides - metabolism; thrombin; trypsin
• ISSN: 1075-2617; 1099-1387
• DOI: 10.1002/(SICI)1099-1387(199908)5:8<352::AID-PSC207>3.0.CO;2-O

Lys(NH2)‐containing peptides were subjected to various proteolytic enzymes which were selected for their well‐documented specificity for arginyl and/or lysyl peptide bonds. Lys(NH2)‐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(NH2)‐containing peptides were incubated in diluted human serum, suggesting that the replacement of Arg or Lys by Lys(NH2) could be used to increase the stability of peptides in vivo. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.