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  • Title: Structure-function studies in a series of carboxyl-terminal octapeptide analogues of anaphylatoxin C5a.
    Author: Kawai M, Quincy DA, Lane B, Mollison KW, Or YS, Luly JR, Carter GW.
    Journal: J Med Chem; 1992 Jan 24; 35(2):220-3. PubMed ID: 1732540.
    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.
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