Using Peptide Arrays To Discover the Sequence-Specific Acetylation of the Histidine-Tyrosine Dyad.,Biochemistry

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Using Peptide Arrays To Discover the Sequence-Specific Acetylation of the Histidine-Tyrosine Dyad.
Biochemistry ( IF 2.9 ) Pub Date : 2019-03-12 , DOI: 10.1021/acs.biochem.9b00022
Lindsey C Szymczak ₁ , Milan Mrksich _{1,

2}

Affiliation

Reactions that can selectively modify amino acid sequences within peptides and proteins are important for preparing protein reagents, immobilizing proteins, and making antibody-drug conjugates. The development of new reactions often begins with known chemistries and optimizes yields using a small set of peptide reactants. This article describes the use of peptide arrays and self-assembled monolayers for matrix-assisted laser desorption/ionization mass spectrometry (SAMDI-MS) to discover and characterize unanticipated sequence-selective reactions of peptides. This work reports the selective acetylation of HY (histidine-tyrosine) and YH (tyrosine-histidine) dyads when treated with acetic anhydride in aqueous conditions. More broadly, this example illustrates the benefits of using peptide arrays and a label-free analysis method to discover peptide-modifying reactions and gain mechanistic insight into their sequence specificity.

中文翻译：

使用肽阵列发现组氨酸-酪氨酸二聚体的序列特异性乙酰化。

可以选择性地修饰肽和蛋白质内氨基酸序列的反应对于制备蛋白质试剂，固定蛋白质和制备抗体-药物偶联物很重要。新反应的开发通常从已知的化学方法开始，并使用少量的肽反应物来优化产率。本文介绍了将肽阵列和自组装单分子膜用于基质辅助激光解吸/电离质谱（SAMDI-MS）来发现和表征肽的意外序列选择性反应的方法。这项工作报告了在水性条件下用乙酸酐处理时，HY（组氨酸-酪氨酸）和YH（酪氨酸-组氨酸）二联体的选择性乙酰化作用。更广泛地，

更新日期：2019-02-28

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