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Issue 4, 2015
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The natural product brartemicin is a high affinity ligand for the carbohydrate-recognition domain of the macrophage receptor mincle

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Abstract

We demonstrate that the natural product brartemicin, a newly discovered inhibitor of cancer cell invasion, is a high-affinity ligand of the carbohydrate-recognition domain (CRD) of the C-type lectin mincle. Recent studies have revealed that mincle is a key macrophage receptor for the mycobacterial virulence factor trehalose dimycolate (TDM), which is a glycolipid component of the mycobacterial cell wall. Major uncertainties, however, remain concerning the mechanism of TDM-binding and subsequent signal transduction as well as interplay of potential co-receptors. Due to the lipid nature of TDM, functional studies are difficult and soluble mincle-ligands are therefore of significant interest. Brartemicin, together with designed analogs also presented in this paper, may thus serve as useful molecular probes for future studies of mincle. Through computational studies, we further provide an insight into the probable mode of binding of brartemicin.

Graphical abstract: The natural product brartemicin is a high affinity ligand for the carbohydrate-recognition domain of the macrophage receptor mincle

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Publication details

The article was received on 10 Nov 2014, accepted on 19 Dec 2014 and first published on 23 Dec 2014


Article type: Concise Article
DOI: 10.1039/C4MD00512K
Citation: Med. Chem. Commun., 2015,6, 647-652
  • Open access: Creative Commons BY license
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    The natural product brartemicin is a high affinity ligand for the carbohydrate-recognition domain of the macrophage receptor mincle

    K. M. Jacobsen, U. B. Keiding, L. L. Clement, E. S. Schaffert, N. D. S. Rambaruth, M. Johannsen, K. Drickamer and T. B. Poulsen, Med. Chem. Commun., 2015, 6, 647
    DOI: 10.1039/C4MD00512K

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