Technicians Training Laboratory, Institute of Chemical Sciences and Engineering (ISIC-GE), Ecole Polytechnique Fédérale de Lausanne, Lausanne CH-1015, Switzerland.
Bioorg Med Chem. 2011 May 1;19(9):2879-87. doi: 10.1016/j.bmc.2011.03.047. Epub 2011 Apr 8.
We described herein the synthesis of second generation glycopeptide dendrimers G2a-g presenting variable amino acids placed internally into the multivalent scaffold. The effect of such structural modulation on recognition processes by Concanavalin A (Con A), was then estimated by enhanced-sensitivity Enzyme-Linked Lectin Assay (ELLA). In a complementary study, glycopeptide dendrons of different valencies and including a l-cysteine residue before the dendritic core (G0SH, G1SH and G2SH), were also synthesized and homodimerized. Then, the disulfide-containing glycopeptide dendrimers generated by this convergent approach (G0(2)S(2), G1(2)S(2) and G2(2)S(2)) were used as Con A inhibitors and assayed by ELLA.
我们在此描述了第二代糖肽树状大分子 G2a-g 的合成，它们展示了可变的氨基酸，这些氨基酸被放置在多价支架的内部。然后，通过增强敏感性的酶联凝集素测定法（ELLA）来评估这种结构修饰对伴刀豆球蛋白 A（Con A）识别过程的影响。在一项补充研究中，还合成了不同价数的糖肽树突并包含一个在树突核心前的 l-半胱氨酸残基（G0SH、G1SH 和 G2SH），并进行了同源二聚化。然后，通过这种收敛方法生成的含二硫键的糖肽树状大分子（G0(2)S(2)、G1(2)S(2) 和 G2(2)S(2)）被用作 Con A 抑制剂，并通过 ELLA 进行测定。
