覆盖着生物分子机器"Chaperonin GroEL"的ATP响应纳米粒子
Hao K Shen1, Kiyoshi Morishita1,2, P K Hashim1
1Department of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8656, Japan.
Angewandte Chemie (International ed. in English)
|May 27, 2023
概括
我们开发了一种具有ATP反应的纳米颗粒,涂上了护卫蛋白GroEL. 这些GroEL纳米颗粒捕获和释放变质蛋白质作为对ATP的反应,显示出增强的ATPase活性.
科学领域:
- 生物技术是生物技术.
- 纳米技术纳米技术
- 生物化学 生物化学
背景情况:
- 像GroEL这样的Chaperonin蛋白质是蛋白质折叠的重要分子机器.
- 开发具有生物分子组件的功能纳米材料是研究的一个关键领域.
研究的目的:
- 为了创建一个ATP-响应的纳米颗粒功能化与 chaperonin 蛋白 GroEL.
- 为了研究GroEL-纳米粒子结合物的蛋白质结合和释放能力.
- 为了评估固定GroEL的ATPase活性.
主要方法:
- 通过DNA杂交合成GroEL功能化黄金纳米粒子 (GroEL NP).
- 使用传输电子显微镜 (TEM) 和冷TEM进行结构性表征.
- 检测蛋白质的捕获和释放,以应对ATP.
- 测量ATPase活动.
主要成果:
- 成功合成了GroEL NP,GroEL覆盖了纳米粒子表面.
- 证明了ATP依赖的脱绿色光蛋白 (GFP) 的捕获和释放.
- 与对照组相比,在GroEL NP中观察到每GroEL单位显著增强的ATPase活性.
- 证实了代扩展的潜力,以创建多层纳米粒子.
结论:
- GroEL NP 是一种具有保留 chaperonin 功能的新型 ATP 响应性纳米材料.
- 增强的ATPase活性表明固定GroEL的性能得到了改善.
- 这个平台有可能用于蛋白质重新折叠和向药物输送.
相关概念视频
Molecular Chaperones and Protein Folding
18.1K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
18.1K
Pinching-off of Coated Vesicles
3.2K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.2K
Clathrin Coated Vesicles
7.1K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
7.1K
Energy to Drive Translocation
2.1K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...
2.1K
ATP Synthase: Structure
12.7K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
12.7K
Bacterial Protein Maturation
41
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
41


