Investigation of peptide stability upon hydrolysis by of fragments of the organs of the gastrointestinal tract of rats

The hydrolytic stability of a range of cyclic tripeptides, including the therapeutically important dalargin and stemokin, as well as peptides modified by ibuprofen and aspirin, has been studied. The first two experimental systems used utilized purified enzymes (pepsin, trypsin, and chymotrypsin), wh...

Full description

Saved in:
Bibliographic Details
Published in:Russian journal of bioorganic chemistry 2010-11, Vol.36 (6), p.690-695
Main Authors: Akimov, M. G, Nazimov, I. V, Gretskaya, N. M, Deigin, V. I, Bezuglov, V. V
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
dalargin
hemopressin
hydrolysis
intestine
Life Sciences
Organic Chemistry
peptides
stemokin
stomach
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The hydrolytic stability of a range of cyclic tripeptides, including the therapeutically important dalargin and stemokin, as well as peptides modified by ibuprofen and aspirin, has been studied. The first two experimental systems used utilized purified enzymes (pepsin, trypsin, and chymotrypsin), while the second one utilized fragments of the stomach and small intestine of rats. The linear peptides containing only L-amino acid residues were shown to be hydrolyzed by stomach and intestine fragments, although some of these peptides were resistant to hydrolysis by individual enzymes. The peptides containing D-amino acid residues and cyclic peptides were stable under all of the conditions used, but the peptides modified by aspirin lost the acetyl group of the aspirin moiety in acidic media, this process being accelerated in the presence of pepsin.
ISSN:1068-1620
1608-330X
DOI:10.1134/S1068162010060038