在纳米粒子支架上的酶组合增强了辅因子循环,并改善了合反应动力学
Joyce C Breger1, Ellen R Goldman1, Kimihiro Susumu2
1Center for Bio/Molecular Science and Engineering Code 6900, U.S. Naval Research Laboratory, Washington, D.C., 20375, USA. Gregory.ellis@nrl.navy.mil.
Nanoscale
|June 5, 2023
概括
当酶在量子点 (QD) 上显示时,酶活性显著增强,促进辅因子循环和酶反应. 这种纳米粒子平台为合成生物学应用提供了新的可能性.
科学领域:
- 生物技术是生物技术.
- 纳米技术纳米技术
- 酶学 是一种酶学.
背景情况:
- 在纳米粒子 (NP) 上的酶固定可以增强活性,并使多酶级联中的道化成为可能.
- 酶辅因子回收对于许多生化过程和合成生物学应用至关重要.
研究的目的:
- 研究当酶在量子点 (QD) 上显示时,酶活性和辅因子循环的增强.
- 探索基于QD的纳米集群的形成及其对酶动力学的影响.
- 评估酶交联在QD纳米集群形成和酶活性中的作用.
主要方法:
- 酶,葡萄糖脱酶 (GDH) 和乳酸脱酶 (LDH) 在半导体量子点 (QD) 上显示.
- 酶动力学测量了辅因子循环 (NAD+到NADH) 和合酶反应.
- 用阿加罗斯凝移动性测试和传输电子显微镜 (TEM) 来表征QD-酶纳米集群.
- 阻断被用来控制QD的酶交叉链接,并评估其对酶活性的影响.
主要成果:
- 在QD上显示GDH,大约增加了5倍的葡萄糖驱动的NAD+减少.
- 在QD纳米集群中合GDH和LDH,增加了乳酸盐转化为酸盐的速度.
- TEM和凝测定证实了QDs的酶介导组装和交叉链接到纳米集群中.
- 阻断QD的酶交叉链接导致单个酶活性进一步增强,高达GDH的10倍增加.
结论:
- 量子点作为增强酶动力学和辅因子循环的有效平台.
- 酶交叉连接影响纳米集群的形成和酶活性,阻断交叉连接可能会增加个体酶的效率.
- 这些发现对基于酶的催化,辅因子再生和无细胞合成生物学有影响.
更多相关视频
09:02Using Polystyrene-block-polyacrylic acid-coated Metal Nanoparticles as Monomers for Their Homo- and Co-polymerization
Published on: July 9, 2015
12.3K
06:57Rapid, Scalable Assembly and Loading of Bioactive Proteins and Immunostimulants into Diverse Synthetic Nanocarriers Via Flash Nanoprecipitation
Published on: August 11, 2018
7.9K
相关概念视频
Protein Complex Assembly
10.7K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.7K
Introduction to Mechanisms of Enzyme Catalysis
8.3K
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
8.3K
Cofactors and Coenzymes
82.7K
Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
82.7K
Assembly of Cytoskeletal Filaments
21.2K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
21.2K
Enzymes
82.0K
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
82.0K
