Neutrophil activation by monomeric interleukin-8
K Rajarathnam, BD Sykes, CM Kay, B Dewald… - Science, 1994 - science.org
K Rajarathnam, BD Sykes, CM Kay, B Dewald, T Geiser, M Baggiolini, I Clark-Lewis
Science, 1994•science.orgInterleukin-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 …
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 …
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.
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