Development of glycopeptide array aiming for diagnosis of infectious diseases

合成了具有56种N-乙酰氨基半乳糖(GalNAc)残基的MUC2粘蛋白(Glyco)多肽，并将其固定在平板上。用ELISA法测定植物凝集素VVA-B4与GalNAc结合的MUC2多肽的亲和力。结果表明，这种亲和力是由GalNAc在多肽上的附着位置决定的。成功研制了GalNAc连接的MUC2多肽平板，这使得测量寄生虫凝集素与GalNAc连接的MUC2多肽的亲和力成为可能。

MUC2 mucin (glyco)peptides with fifty-six patterns of N-acetylgalactosamine (GalNAc) residue attachment were synthesized and immobilized on the plate. Binding affinities of VVA-B4, a plant lectin, toward GalNAc attached MUC2 peptides were measured using ELISA. The results suggested that the affinity was defined by the sites of GalNAc attachment on the peptides. The plate with GalNAc attached MUC2 peptides was successfully developed and this made possible for measuring the affinities of parasite lectins toward GalNAc attached MUC2 peptides.