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Chemoenzymatic synthesis of neoglycoproteins driven by the assessment of protein surface reactivity

机译：评估蛋白质表面反应性驱动的新糖化学合成

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摘要

In this paper a series of 2-iminomethoxyethyl mannose-based mono-and disaccharides have been synthesized by a chemoenzymatic approach and used in coupling reactions with epsilon-amino groups of lysine residues in a model protein (ribonuclease A, RNase A) to give semisynthetic neoglycoconjugates. In order to study the influence of structure of the glycans on the conjugation outcomes, an accurate characterization of the prepared neoglycoproteins was performed by a combination of ESI-MS and LC-MS analytical methods. The analyses of the chymotryptic digests of the all neoglycoconjugates revealed six Lys-glycosylation sites with a the following order of lysine reactivity: Lys 1 Lys 91 congruent to Lys 31 > Lys 61 congruent to Lys 66. A computational analysis of the reactivity of each lysine residue has been also carried out considering several parameters (amino acids surface exposure and pK(a), protein flexibility). The in silico evaluation seems to confirm the order in lysine reactivity resulting from proteomic analysis.
机译：在本文中，通过化学酶法合成了一系列基于2-亚氨基甲氧基乙基甘露糖的单糖和二糖，并用于与模型蛋白（核糖核酸酶A，RNase A）中赖氨酸残基的ε-氨基偶联反应，得到半合成蛋白。新糖缀合物。为了研究聚糖结构对偶联结果的影响，通过结合ESI-MS和LC-MS分析方法对制备的新糖蛋白进行了准确表征。对所有新糖缀合物的胰凝乳蛋白酶消化物的分析显示六个Lys-糖基化位点，其赖氨酸反应性按以下顺序排列：Lys 1 Lys 91与Lys 31一致> Lys 61与Lys 66一致。还考虑了几个参数（氨基酸表面暴露和pK（a），蛋白质柔韧性）对每个赖氨酸残基进行了分析。电子计算机评估似乎证实了由蛋白质组学分析得出的赖氨酸反应性顺序。

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