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Tryptic hydrolysis of hGH‐RH(1‐29)‐NH 2 analogues containing Lys or Orn in positions 12 and 21
Author(s) -
Witkowska Ewa,
Orłowska Alicja,
Sagan Bru,
Smoluch Marek,
Izdebski Jan
Publication year - 2001
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/psc.316
Subject(s) - chemistry , hydrolysis , trypsin , cleavage (geology) , peptide , amino acid , peptide bond , amino acid residue , stereochemistry , peptide sequence , biochemistry , enzyme , biology , paleontology , fracture (geology) , gene
Two analogues of the 29 amino acid sequence of human growth hormone‐releasing hormone, namely [Nle 27 ]hGH‐RH(1‐29)‐NH 2 and [Orn 12,21 ,Nle 27 ]hGH‐RH(1‐29)‐NH 2 , have been synthesized and subjected to digestion by trypsin. The course of degradation was followed using RP‐HPLC and ESI‐MS. Several intermediates and final products of degradation were identified and conclusions regarding the rate of cleavages at different positions occupied by Lys and Arg residues were drawn. The analogue containing ornithine was found to be less susceptible to hydrolysis by trypsin: the 12‐13 and 21‐22 peptide bonds were completely resistant to the cleavage. The results show that by replacing Lys with Orn, a possibility exists to design new peptides, which could be more stable in biological fluids. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.