折叠体囊的疏水性崩促使在水性酸溶液中形成皮科莫尔水平的化物结合
Yuran Hua1, Yun Liu, Chun-Hsing Chen
1Department of Chemistry, Indiana University , 800 East Kirkwood Avenue, Bloomington, Indiana 47405, United States.
Journal of the American Chemical Society
|September 14, 2013
概括
研究人员开发了一种新型的aryl-triazole折叠剂,该折叠剂利用疏水性相互作用将水友化离子结合到水中. 这种水辅助策略为水环境中的宿主-客化学提供了一种新的方法.
科学领域:
- 超分子化学 超分子化学
- 有机化学 有机化学
- 生物模拟化学 生物模拟化学
背景情况:
- 水性环境对宿主和客人的化学反应构成挑战,特别是对充电的客人来说.
- 疏水性结合对非极地客是有效的,但对化物等疏水性阴离子需要补充策略.
- 蛋白质利用特定的机制来结合水友性客体,这在人造受体中不太常见.
研究的目的:
- 通过使用人工受体在水性介质中结合水友化离子的替代机制.
- 为了证明水相互作用在组织和稳定离子提取的折叠器中的作用.
- 探索适用于其他水友性客人的宿主-客人化学的水辅助策略.
主要方法:
- 设计和合成一个阿里尔-二醇折叠剂.
- 研究不同水性乙尼特溶液中与离子的折叠分子复合.
- 使用光谱和结合研究对双螺旋复合体稳定性和微环境的表征.
主要成果:
- 疏水性相互作用稳定了阿里尔-二醇折叠剂,使得疏水性化物离子可以提取.
- 形成一个双螺旋复合体,埋葬 π 表面,并为结合创造一个不含溶剂的微环境.
- 在25%的水中观察到对化物离子的显著亲和力 (log β2 = 12.6),在50%的水中保持强烈的亲和力 (log β2 = 13.0).
结论:
- 可以利用疏水性相互作用来组织人造受体,以在水溶液中结合水友性阴离子.
- 开发的阿里尔-三折叠剂表现出一种水辅助的结合策略,模仿蛋白质类机制.
- 这种方法有可能用于设计用于绑定各种水友性客体的非生物折叠体.
相关概念视频
03:00Molecular Chaperones and Protein Folding
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...
01:01Acid Halides to Carboxylic Acids: Hydrolysis
Hydrolysis of acid halides is a nucleophilic acyl substitution reaction in which acid halides react with water to give carboxylic acids. The reaction occurs readily and does not require acid or a base catalyst.
As shown below, the mechanism involves a nucleophilic attack by water at the carbonyl carbon to form a tetrahedral intermediate. This is followed by the reformation of the carbon–oxygen π bond along with the departure of a halide ion. A final proton transfer step yields carboxylic acid...
As shown below, the mechanism involves a nucleophilic attack by water at the carbonyl carbon to form a tetrahedral intermediate. This is followed by the reformation of the carbon–oxygen π bond along with the departure of a halide ion. A final proton transfer step yields carboxylic acid...
01:30Micelles
Micelle formation is an intricate process that hinges on the properties of amphiphilic or amphipathic molecules and the conditions of the system in which they are found. Amphiphilic molecules, which have both hydrophilic (water-attracting) and hydrophobic (water-repelling) parts, play a critical role in this process.In aqueous environments, these molecules arrange themselves such that their hydrophilic heads are turned towards the water phase, while their hydrophobic tails are oriented away...
01:32Pinching-off of Coated Vesicles
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...