1993
DOI: 10.1023/a:1018953309913
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Abstract: The determination of peptide stability in human serum (HS) or plasma constitutes a powerful screening assay for eliminating unstable peptides from further development. Herein we report on the stability in HS of several major histocompatibility complex (MHC)-binding peptides. Some of these peptides are in development for the novel treatment of selected autoimmune disorders such as rheumatoid arthritis and insulin-dependent diabetes. For most of the l-amino acid peptides studied, the predominant degradation mech… Show more

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Cited by 174 publications
(57 citation statements)
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“…Serum generally degrades peptides very quickly24 due to the presence of multiple proteases with differing specificity (e.g., thrombin, plasmin, and kallikrein). In line with that view, linear GiBP is undetectable at the first time point after incubation (t 1/2 < 1 min) and cycGiBP shows a half-life of ~20 minutes.…”
Section: Resultsmentioning
confidence: 99%
“…Serum generally degrades peptides very quickly24 due to the presence of multiple proteases with differing specificity (e.g., thrombin, plasmin, and kallikrein). In line with that view, linear GiBP is undetectable at the first time point after incubation (t 1/2 < 1 min) and cycGiBP shows a half-life of ~20 minutes.…”
Section: Resultsmentioning
confidence: 99%
“…[23][24][25]. Triplicate samples of native and cyclic peptides were assayed simultaneously at a concentration of 20 M. At 0, 4, 8, 12, 16, and 24 h, 200 l of the mixture was removed and added to 100 l of 15% aqueous trichloroacetic acid to precipitate serum proteins.…”
Section: Methodsmentioning
confidence: 99%
“…24 and see below). The non-natural residues we used (D-amino acids, N-methyl-amino acids, and Aib) are efficient inhibitors of exopeptidase (aminopeptidase and ACE) activities (35). We may reasonably postulate that the disubstituted analogues should also be peptidase-resistant in vivo (18).…”
Section: A1 and Its Substituted Analoguesmentioning
confidence: 99%