用于重组蛋白质和抗体的钇寡肽标签的设计和NMR结构测定

IF 0.9 Q4 CHEMISTRY, MULTIDISCIPLINARY
Marcela Múdra, M. Breza, Lucia Lintnerová, J. Filo, J. Bauer
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引用次数: 0

摘要

摘要描述了一种由天然氨基酸序列组成的新型钇(III)标签的设计策略。这些标签长度为4-6个氨基酸,由天冬氨酸和谷氨酸组成。天然氨基酸的使用将允许这些寡肽在DNA水平上被整合到重组蛋白中,使蛋白质在分离后被Y(III)标记。这允许放射性核素或重原子与蛋白质结合,而不需要进一步的合成修饰。基于量子化学计算,设计了能够在稳定配合物中螯合Y(III)的合适肽。通过等温滴定量热法测试了这些肽形成的配合物的稳定性,给出了微摩尔范围内的解离常数。结合核磁共振实验和量子化学计算推断出最紧密结合的复合物的可能结构。这个结构将作为未来优化的基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The design and NMR structure determination of yttrium-oligopeptide tags for recombinant proteins and antibodies
Abstract A strategy for the design of new yttrium(III) tags consisting of sequences of naturally occurring amino acids is described. These tags are 4–6 amino acids in length and consist of aspartic and glutamic acids. The use of natural amino acids would allow these oligopeptides to be incorporated into recombinant proteins at the DNA level, enabling the protein to be Y(III)-labelled after protein isolation. This allows a radionuclide or heavy atom to be associated with the protein without the necessity of further synthetic modification. Suitable peptides able to chelate Y(III) in stable complexes were designed based on quantum-chemical calculations. The stability of complexes formed by these peptides was tested by isothermal titration calorimetry, giving dissociation constants in the micromolar range. The likely structure of the most tightly bound complex was inferred from a combination of NMR experiments and quantum-chemical calculations. This structure will serve as the basis for future optimizations.
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来源期刊
Acta Chimica Slovaca
Acta Chimica Slovaca CHEMISTRY, MULTIDISCIPLINARY-
自引率
12.50%
发文量
11
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