聚乙二醇化天冬酰胺酶的特性：来自大型聚乙二醇化治疗药物的 NMR 分析的新机遇。
Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics.
机构信息
Magnetic Resonance Center (CERM), University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di, Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.
Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy.
出版信息
Chemistry. 2019 Feb 6;25(8):1984-1991. doi: 10.1002/chem.201804488. Epub 2019 Jan 9.
Resonance assignment and structural characterization of pharmacologically relevant proteins promise to improve understanding and safety of these proteins by rational design. However, the PEG coating that is used to evade the immune system also causes these molecules to "evade" the standard structural biology methodologies. We here demonstrate that it is possible to obtain the resonance assignment and a reliable structural model of large PEGylated proteins through an integrated approach encompassing NMR and X-ray crystallography.
通过合理设计，对药物相关蛋白进行共振分配和结构特征分析有望提高对这些蛋白的认识并提升其安全性。然而，用于逃避免疫系统的聚乙二醇（PEG）涂层也使这些分子“逃避”了标准的结构生物学方法。我们在此证明，通过将 NMR 和 X 射线晶体学相结合的综合方法，有可能获得大的 PEG 化蛋白的共振分配和可靠的结构模型。
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