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A PIM2 analogue suppresses allergic airway disease

TitleA PIM2 analogue suppresses allergic airway disease
Publication TypeJournal Article
Year of Publication2011
AuthorsHarper, J. L., Hayman C. M., Larsen D. S., Painter G. F., and Singh-Gill G.
IRL TeamCarbohydrate Chemistry
JournalBioorganic and Medicinal Chemistry
Volume19
Pagination917-925
Keywords2 o (1, 2 o (4 methoxybenzyl)glycerol 14, 2 o benzoyl 1, 2 o distearoyl sn glycero 3 phoshoryl) 1, 3, 3 bis (2, 3 bis (2 o methoxycetyl alpha dextro mannopyranosyl)glycerol 26, 3 bis (3, 3 bis o (2, 3 bis o (alpha dextro mannopyranosyl)glycerol 4, 4, 5 tetra o benzyl alpha dextro mannopyranosyl) 2 o (4 methoxybenzyl)glycerol 20, 5 tetra o benzyl alpha dextro mannopyranosyl)glycerol 10, 5 tri o benzyl 1, 5 tri o benzyl a dextro mannopyranosyl) 2 o (4 methoxybenzyl)glycerol 19, 6 tetra o benzyl a dextro mannopyranosyl) glycerol 6, 6 tetra O benzyl a dextro mannopyranosyl)glycerol 10, 6 tetra o benzyl alpha dextro mannopyranosyl)glycerol 13, 6 tetra o benzyl alpha dextro mannopyranosyl)glycerol 7, 6 tetra o benzyl dextro mannopyranosyl)glycerol 9, Administration, allergic asthma, animal, animal cell, animal experiment, animal model, Animals, Anti-Allergic Agents, antiallergic agent, article, Asthma, carbohydrate derivative, cell activity, chemistry, controlled study, drug, drug structure
Abstract Two approaches for the synthesis of a phosphatidylinositol dimannoside (PIM2) analogue 4 that mimics the suppressive activity of natural PIMs and also synthetic PIM2 have been developed. This analogue, where the inositol core was replaced by glycerol, was tested for its ability to suppress cellular inflammation in a mouse model of allergic asthma and shown to be effective in suppressing airway eosinophilia. Suppression of all inflammatory cells monitored was observed, indicating a general blockade of cellular activity. These data indicate that the inositol core is not essential for this suppressive activity. © 2010 Elsevier Ltd. All rights reserved.
URLhttp://www.scopus.com/inward/record.url?eid=2-s2.0-78651473169&partnerID=40&md5=86f38235e6d56dbff0f33a6a3f6f3c3e
DOI10.1016/j.bmc.2010.11.058