Reactivity of Lys(NH2)-containing peptides toward endopeptidases.
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.
Samson
F
F
UMR 8525 CNRS, Institut de Biologie de Lille-Institut Pasteur de Lille, France.
Bonnet
D
D
Rommens
C
C
Gras-Masse
H
H
Melnyk
O
O
D000421:Alcaligenes / Q000201:enzymology; D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D008239:Lysine / Q000378:metabolism*; D010455:Peptides / Q000097:blood / Q000737:chemistry / Q000378:metabolism*
D010455:Peptides; D010450:Endopeptidases; D008239:Lysine