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

@article{Kawai1992StructurefunctionSI,
  title={Structure-function studies in a series of carboxyl-terminal octapeptide analogues of anaphylatoxin C5a.},
  author={Megumi Kawai and David A. Quincy and Benjamin C Lane and Karl W. Mollison and Yat Sun Or and Jay R Luly and George W. Carter},
  journal={Journal of medicinal chemistry},
  year={1992},
  volume={35 2},
  pages={220-3}
}
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… CONTINUE READING