—Iron catalysts diversify amino acids and peptides “New method mimics peptide-synthesis enzyme complexes found in microorganisms” To create peptides with diverse types of bioactivity, microorganisms use multienzyme complexes called nonribosomal peptide synthetases (NRPSs). For example, bacteria make the antibiotic vancomycin this way. Iron-based enzymes in NRPSs oxidize and modify amino acids both before and after the complexes assemble the amino acids into peptides. A new technique enables chemists to diversify amino acids and peptides the way that NRPSs do. The approach, its developers say, could make it easier to discover new peptide-based therapeutics, dozens of which are already on the market or in testing. Chemists aren’t as good at diversifying peptides as microbes are. Researchers often must synthesize peptides with modified amino acids from scratch, a laborious and time-consuming process. There are a few ways to oxidize amino acids to functionalize the molecules, but these techniques are frequently difficult, sometimes alter amino acid stereochemistry, and have limited ability to modify amino acids already in peptides.
by Stu Borman |
August 04, 2016