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J Med Chem. 1992 Jan 24;35(2):220-3.

Structure-function studies in a series of carboxyl-terminal octapeptide analogues of anaphylatoxin C5a.

Author information

1
Pharmaceutical Products Division, Abbott Laboratories, Abbott Park, Illinois 60064.

Abstract

The synthesis and structure-activity relationships of C-terminal octapeptide analogues of anaphylatoxin C5a have been studied. The introduction of hydrophobic amino acids into the N-acetylated native octapeptide (N-Ac-His-Lys-Asp-Met-Gln-Leu-Gly-Arg-OH) (1) has led to an analogue with 100 times more activity than the native octapeptide in inhibiting the binding of 125I-labeled anaphylatoxin C5a to human neutrophil membrane receptors. The observed apparent binding Ki's for the compounds (8-10) are in the range of 1-3 microM, and they possess nearly full agonist activity, despite the fact that these analogues are one-eighth or -ninth the size of the natural ligand anaphylatoxin C5a.

PMID:
1732540
DOI:
10.1021/jm00080a004
[Indexed for MEDLINE]

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