O-Methylation, commonly found in synthesis of secondary metabolites of plants and micro-organisms, appears to transfer a methyl group to the hydroxyl group of the recipient which increases the hydrophobicity of the recipient. O-Methyltransferase (OMT), , was isolated and characterized from Streptomyces avermitilis MA-4680. Its amino acid sequence showed 68% similarity with antibiotic C-1027 OMT and 53% similarity with the carminomycin 4-OMT. was expressed in E. coli as a His-tag fusion protein and showed that the methyl was transferred onto the 7-hydroxyl group of the isoflavones, daidzein and genistein, and the flavones, kaempferol and quercetin, as well as the flavanone naringenin. NMR and liquid chromatography-mass spectrometry were used to confirm the location of the methyl group on the recipient compound of naringenin, which was biotransformed into sakuranetin by E. coli transformant expressing (E. coli Sa-2). Therefore, E. coli Sa-2 would be used for the synthesis of the antifungal flavonoid, sakuranetin, through biotransformation.
Significant efforts have been devoted to the development of nanoparticular delivering systems targeting tumors. However, clinical application of nanoparticles is hampered by insufficient size homogeneity, difficulties in reproducible synthesis and manufacturing, frequent high uptake in the liver, systemic toxicity of the carriers (particularly for inorganic nanoparticles), and insufficient selectivity for tumor cells. We have found that properly modified synthetic analogs of transmembrane domains of membrane proteins can self-assemble into remarkably uniform spherical nanoparticles with innate biological activity. Self-assembly is driven by a structural transition of the peptide that adopts predominantly a beta-hairpin conformation in aqueous solutions, but folds into an alpha-helix upon spontaneous fusion of the nanoparticles with cell membrane. A 24-amino acid peptide corresponding to the second transmembrane helix of the CXCR4 forms self-assembled particles that inhibit CXCR4 function in vitro and hamper CXCR4-dependent tumor metastasis in vivo. Furthermore, such nanoparticles can encapsulate hydrophobic drugs, thus providing a delivery system with the potential for dual biological activity.virus-like particles | CXCL12 | cancer | undruggable target
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