Neutrophil activation by monomeric interleukin-8

Krishnakumar Rajarathnam, Brian D. Sykes, Cyril M. Kay, Beatrice Dewald, Thomas Geiser, Marco Baggiolini, Ian Clark-Lewis

Research output: Contribution to journalArticle

269 Scopus citations


Interleukin-8 (IL-8), a pro-inflammatory protein, has been shown by nuclear magnetic resonance (NMR) and x-ray techniques to exist as a homodimer. An IL-8 analog was chemically synthesized, with the amide nitrogen of leucine-25 methylated to selectively block formation of hydrogen bonds between monomers and thereby prevent dimerization. This analog was shown to be a monomer, as assessed by analytical ultracentrifugation and NMR. Nevertheless, it was equivalent to IL-8 in assays of neutrophil activation, which indicates that the monomer is a functional form of IL-8.

Original languageEnglish (US)
Pages (from-to)90-92
Number of pages3
Issue number5155
StatePublished - Apr 1 1994
Externally publishedYes

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    Rajarathnam, K., Sykes, B. D., Kay, C. M., Dewald, B., Geiser, T., Baggiolini, M., & Clark-Lewis, I. (1994). Neutrophil activation by monomeric interleukin-8. Science, 264(5155), 90-92.