嗜热菌的热稳定性苯乙酸降解蛋白 TtPaaI 作为蛋白质四价展示的支架。

IF 1.4 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Protein expression and purification Pub Date : 2024-11-12 DOI:10.1016/j.pep.2024.106623

Aleksandra Chorążewska, Darragh Regan, Marta Kalka, Krzysztof Ciura, Natalia Porębska, Łukasz Opaliński

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引用次数: 0

摘要

自然界中的许多蛋白质都需要低聚才能充分发挥其活性。此外，天然和人工蛋白质的功能可以通过改变其低聚物状态进行调整，从而开发出与生物技术相关的生物大分子。从天然来源和重新设计的低聚物支架可以改变生物大分子的低聚物状态和价态。在本报告中，我们探究了嗜热菌（Thermus thermophilus）的恒温苯乙酸降解蛋白酰基-CoA（TtPaaI）的支架化潜力。我们设计并成功制备了 TtPaaI（支架）与 galectin-7（配体）的融合蛋白，galectin-7 是一种与人类疾病有关的多功能凝集素（配体）。

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Thermostable phenylacetic acid degradation protein TtPaaI from Thermus thermophilus as a scaffold for tetravalent display of proteins

Numerous proteins in nature strictly require oligomerization for their full activity. Moreover, the function of natural and artificial proteins can me adjusted by altering their oligomeric state, leading to development of biotechnologically-relevant biomacromolecules. Oligomerization scaffolds from natural sources and designed de novo enable shuffling the oligomeric state and valency of biomacromolecules. In this report we probed the scaffolding potential of the thermostable phenylacetic acid degradation protein acyl-CoA from Thermus thermophilus (TtPaaI). We designed and successfully produced the fusion protein between TtPaaI (scaffold) and galectin-7, a multifunctional lectin implicated in human diseases (ligand) and demonstrated that TtPaaI can serve as a framework for functional multivalent display of ligands.

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来源期刊

Protein expression and purification 生物-生化研究方法

CiteScore

3.70

自引率

6.20%

发文量

120

审稿时长

32 days

期刊介绍： Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.