Synthesis of glycopeptide dendrimers, dimerization and affinity for Concanavalin A.
Synthesis of glycopeptide dendrimers, dimerization and affinity for Concanavalin A.
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DOI：
10.1016/j.bmc.2011.03.047
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发表时间：
2011-05
影响因子：
3.5
通讯作者：
Ronan Euzen;J. Reymond
中科院分区：
文献类型：
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作者：
Ronan Euzen;J. Reymond
在这里，我们描述了第二代糖肽树枝状大分子G2a-G的合成，这些树状大分子将可变氨基酸放入多价支架中。然后用增敏酶联凝集素试验(ELLA)评估这种结构调节对刀豆蛋白A(ConA)识别过程的影响。在一项补充研究中，还合成了不同价态的糖肽树突，包括树突核心前的半胱氨酸残基(G0SH、G1SH和G2SH)，并均二聚。然后，用这种收敛方法生成的含二硫糖肽树枝状大分子(G02S2、G12S2和G22S2)作为ConA抑制剂，并用ELLA进行检测。
We described herein the synthesis of second generation glycopeptide dendrimersG2a–gpresenting 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 al-cysteine residue before the dendritic core (G0SH,G1SHandG2SH), were also synthesized and homodimerized. Then, the disulfide-containing glycopeptide dendrimers generated by this convergent approach (G02S2,G12S2andG22S2) were used as Con A inhibitors and assayed by ELLA.