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pubmed:abstractText |
An extract from the fungus Emericella aurantiobrunnea was found to compete with macrophage inflammatory protein (MIP)-1alpha for binding to human CCR5 in a scintillation proximity assay (SPA). Bioassay-guided fractionation led to the isolation of variecolin (1) and variecolol (2), which had IC50 values of 9 and 32 microM, respectively. An X-ray crystal structure of variecolin (1) was obtained for the first time. Also isolated were four new inactive analogues, emericolin A (3), B (4), C (5), and D (6), and the relative stereochemistry of these compounds was determined by NMR methods using ROESY spectra and 1H/1H coupling constants.
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