Description: The majority of drugs on the market have a biosynthetic origin. A significant portion of these biosynthetic drugs are produced by nonribosomal peptide synthetases (NRPS), large multi-modular enzymes found in various bacterial and fungal species. NRPS synthesize structurally and functionally diverse biologically active peptides that often have unique modifications (such as cyclization, oxidation, methylations, etc.), and are a source of antibacterial, antifungal, and anticancer drugs (examples include cyclosporine A and vancomycin). Their products are highly specific and can contain non-standard or synthetic amino acids, but are also difficult to create and optimize through synthetic chemistry. Queen’s iGEM aims to accomplish three goals: improve tagging of NRPS products for high-throughput screening to assess biochemical activity, append functional groups such as halogens to NRPS products by incorporating cis tailoring domains via homologous recombination, and performing in silico mutagenesis of NRPS domains to alter their substrate specificity for incorporation of non-standard amino acids.
Collaboration details:
Year: 2016Visit Wiki
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Updated at: 8/9/16