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

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.

journal_name

J Med Chem

journal_title

Journal of medicinal chemistry

authors

Kawai M,Quincy DA,Lane B,Mollison KW,Or YS,Luly JR,Carter GW

doi

10.1021/jm00080a004

subject

Has Abstract

pub_date

1992-01-24 00:00:00

pages

220-3

issue

2

eissn

0022-2623

issn

1520-4804

journal_volume

35

pub_type

杂志文章

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