Gobbo M, Biondi L, Filira F, Scolaro B, Rocchi R, Piek T
Biopolymer Research Centre, C.N.R., Department of Organic Chemistry, University of Padua, Italy.
Int J Pept Protein Res. 1992 Jul;40(1):54-61. doi: 10.1111/j.1399-3011.1992.tb00104.x.
Syntheses are described of some mono- and di-glycosylated analogues of vespulakinin 1. The solid phase procedure, based on the Fmoc chemistry, was used to prepare (Gal alpha)Thr3-vespulakinin 1, (Gal beta)Thr3-vespulakinin 1 and the di-glycosylated analogue ((Gal alpha)Thr3, (Gal alpha)Thr4-vespulakinin 1. The beta-glycosylated derivative was also prepared by the continuous flow variant of the Fmoc polyamide method. The synthesized glycopeptides were purified and characterized by amino acid analysis, optical rotation, analytical HPLC, 1H- and 13C-NMR and FAB-MS. Preliminary pharmacological experiments showed that the carbohydrate-free vespulakinin 1 is less active than bradykinin (about 0.3 times on a molar basis) when tested by guinea pig rectum contraction, and the two monoglycosylated analogues are equiactive (about 0.9 times the bradykinin activity). The most active derivative, the (Gal alpha)Thr3, (Gal alpha)Thr4-vespulakinin 1 analogue, was about 2.5 times as active as bradykinin.
本文描述了黄蜂激肽1的一些单糖基化和二糖基化类似物的合成。基于Fmoc化学的固相合成方法用于制备（Galα）Thr3 - 黄蜂激肽1、（Galβ）Thr3 - 黄蜂激肽1和二糖基化类似物（（Galα）Thr3，（Galα）Thr4 - 黄蜂激肽1）。β - 糖基化衍生物也通过Fmoc聚酰胺方法的连续流动变体来制备。合成的糖肽通过氨基酸分析、旋光、分析型HPLC、1H - 和13C - NMR以及FAB - MS进行纯化和表征。初步药理实验表明，在豚鼠直肠收缩实验中，无糖基化的黄蜂激肽1的活性低于缓激肽（摩尔基础上约为0.3倍），而两种单糖基化类似物具有同等活性（约为缓激肽活性的0.9倍）。活性最高的衍生物，即（Galα）Thr3，（Galα）Thr4 - 黄蜂激肽1类似物，活性约为缓激肽的2.5倍。
