一个单分子G-四重复体,其功能是合成的跨膜Na+载体
Mark S Kaucher1, William A Harrell, Jeffery T Davis
1Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA.
Journal of the American Chemical Society
|January 5, 2006
概括
研究人员创造了一个强大的跨膜 (Na+) 离子输送器,通过对键组件进行共价性修改. 这种新的G-四重复结构有效地将Na+离子穿过细胞膜.
科学领域:
- 超分子化学 超分子化学
- 生物物理化学 生物物理化学
- 膜运输是通过膜运输来实现的.
背景情况:
- 结合组件为分子识别和自我组装提供了潜力.
- 为特定的离子设计人工输送器对于理解生物过程和开发新技术至关重要.
研究的目的:
- 开发一种新型,强大的跨膜 (Na+) 离子输送器.
- 探索用于功能应用的键组件的共价后修改.
主要方法:
- 使用olefin转基因合成,将16个瓜诺辛子单元交叉链接成一个脂友G-四重复结构.
- 在脂膜环境中研究G-四重体的折叠和功能.
- 使用光和23Na核磁共振 (NMR) 测试来评估Na+离子运输活动.
主要成果:
- 通过对瓜诺辛子单元的共价交联成功合成了一个单分子G-四重复合体.
- 证明了修改后的G-四重复在脂膜内折叠.
- 通过光和23Na的NMR测定证实了G-quadruplex强大的跨膜Na+离子输送能力.
结论:
- 键组件的共价后修改可以产生功能生物模拟系统.
- 开发的G-quadruplex作为一个有效的人工Na+离子传送器穿过膜.
- 这项工作为创建具有潜在生物医学应用的复杂分子转运器提供了新的策略.
相关概念视频
G-protein Coupled Receptors
G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
Golgi Matrix Proteins
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
G-protein Coupled Receptors
G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
Multi-pass Transmembrane Proteins and β-barrels
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
G Protein-coupled Receptors
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Activation and Inactivation of G Proteins
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...


