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Selective N-terminal acylation of peptides and proteins with a Gly-His tag sequence

机译:带有Gly-His标签序列的肽和蛋白质的选择性N末端酰化

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Methods for site-selective chemistry on proteins are in high demand for the synthesis of chemically modified biopharmaceuticals, as well as for applications in chemical biology, biosensors and more. Inadvertent N-terminal gluconoylation has been reported during expression of proteins with an N-terminal His tag. Here we report the development of this side-reaction into a general method for highly selective N-terminal acylation of proteins to introduce functional groups. We identify an optimized N-terminal sequence, GHHHn? for the reaction with gluconolactone and 4-methoxyphenyl esters as acylating agents, facilitating the introduction of functionalities in a highly selective and efficient manner. Azides, biotin or a fluorophore are introduced at the N-termini of four unrelated proteins by effective and selective acylation with the 4-methoxyphenyl esters. This Gly-Hisn tag adds the unique capability for highly selective N-terminal chemical acylation of expressed proteins. We anticipate that it can find wide application in chemical biology and for biopharmaceuticals.
机译:对蛋白质进行位点选择化学的方法对化学修饰的生物药物的合成以及在化学生物学,生物传感器等领域的应用非常需要。已经报道了在表达具有N末端His标签的蛋白质的过程中无意中的N末端糖基化。在这里,我们报告这种副反应的发展为蛋白质的高选择性N末端酰化以引入官能团的一般方法。我们确定了优化的N端序列GHHHn?与葡糖酸内酯和4-甲氧基苯基酯作为酰化剂的反应,有助于以高度选择性和有效的方式引入官能团。通过用4-甲氧基苯基酯进行有效和选择性的酰化作用,将叠氮化物,生物素或荧光团引入四个不相关蛋白质的N末端。该Gly-Hisn标签为表达蛋白的高选择性N端化学酰化增加了独特的功能。我们希望它可以在化学生物学和生物制药领域找到广泛的应用。

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