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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Immunoregulatory activity of peptides related to platelet factor 4.

Platelet factor 4 ( PF4), a secreted platelet protein, alleviates concanavalin A-induced immunosuppression in mice. We now find that activity also resides in (i) the C-terminal tridecapeptide of PF4 (P13S), (ii) an analog of this in which arginine replaces the lysine residues and in which the last two amino acids are absent, (iii) the C-terminal 18 amino acids of low-affinity platelet factor 4, which is very similar to P13S, and (iv) peptide fragments of P13S that contain only 5-9 amino acids. P13S treated with fluorescamine to derivatize the free amino groups retained immunoregulatory activity but did not bind to heparin-agarose. The N-terminal and middle portions of PF4, polylysine, protamine, and three unrelated peptides were inactive in this assay.[1]

References

  1. Immunoregulatory activity of peptides related to platelet factor 4. Zucker, M.B., Katz, I.R., Thorbecke, G.J., Milot, D.C., Holt, J. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
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