20 多官能ピペリジンの合成と生物活性 : シアスタチンB類(ポスター発表の部)

抄録

Neuraminidase and sialyltransferase, respectively hydrolysing and transferring N-acetylneuraminic acid in the non-reducing end of carbohydrate chains of glycoproteins and glycolipids, are involved in various biological functions such as immune response, oncogenesis, metastasis of tumors, sperm penetration, viral infection, etc. Siastatin B (1), an inhibitor of neuraminidase, was isolated by H. Umezawa et al. in 1974 from a Streptomyces culture. The total synthesis of siastatin B was achieved in a totally stereospecific fashion based on a chiron strategy, and consequently its absolute configuration elucidated as 2R-acetamido-3R,4S-dihydroxypiperidine-5S-carboxylic acid. Recent experiences in totally synthetic as well as chemically modified analogues (more than 60 compounds), rationally designed species able to mimic N-acetylneuraminic acid in glycoprotein or glycolipid, will be discussed, especially those types which represent an improvement over siastatin B.