Enzymatic synthesis of oligosaccharides using specific sialyltransferases enables single-step glycosylation with high positional and anomeric structural selectivity. The α2,3-sialyltransferase cloned from the marine bacterium Photobacterium sp. JT-ISH-224 has unique and broad acceptor specificity, but this enzyme possesses not only sialyltransferase activity but also sialidase activity. To synthesize sialoside derivative effectively, only sialyltransferase activity is required. We report here that addition of organic solvents was effective to control the sialidase activity and a resulting product was not hydrolyzed. The enzyme was even active in the presence of acetonitrile, ethanol, methanol, or acetone. To determine the suitable concentrations of these organic solvents, only sialyltransferase activity could be allowed, and as a result, the stable synthesis of sialoside could be achieved.Graphical abstractHighlights► α2,3-Sialyltransferase (JT-ISH-224) possesses also sialidase activity. ► The enzyme was even active in the presence of water-soluble organic solvents. ► Water-soluble organic solvents mean acetonitrile, ethanol, methanol, or acetone. ► Only sialyltransferase activity was allowed in the presence of the organic solvents.

Cyclic RGD peptides are potent antagonists for the αvβ3 integrin receptor. In this Letter, microwave-assisted solid-phase synthesis of cyclic RGD peptides is described. In a coupling reaction between Fmoc-Arg(Pbf)-OH and high-loading H-Gly-Trt(2-Cl) resin, multiple coupling reactions were required for completion under the conventional HBTU activation. We found that the use of COMU, a new coupling reagent, under microwave heating to 50 °C accelerated the reaction even inside the resin. This method was applicable to the synthesis of linear pentapeptides, H-Asp(OtBu)-Xxx-Yyy-Arg(Pbf)-Gly-OH (Xxx = d-Phe(p-Br) or d-Tyr, Yyy = Lys(Boc) or MeVal). Cyclization of these peptides followed by deprotection gave the desired cyclic RGD peptides with high purity.