相关实验视频
Updated: May 13, 2025

07:11
Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
2.6K
硫 (IV) 基于化学的和蛋白质晚期修饰
Dongyan Yang1, Zhijun Ruan2, Shiliang He3
1College of Chemistry and Chemical Engineering, Zhongkai University of Agriculture and Engineering, Guangzhou, 510230, China.
Chembiochem : a European journal of chemical biology
|April 16, 2025
概括
新的硫 (IV) 化学使得精确的和蛋白质修饰成为可能,克服了当前方法的局限性. 这一进步为研究生物功能和开发先进的宏分子疗法提供了新的工具.
科学领域:
- 化学生物学 化学生物学
- 生物化学 生物化学
- 药用化学 医学化学
背景情况:
- 对和蛋白质进行精确的化学修饰对于理解结构-活性关系和开发治疗方法至关重要.
- 现有的方法,如不可逆转的共价标签和非自然氨基酸结合,在可逆性,局部调节和生理适应性方面存在局限性.
研究的目的:
- 审查和蛋白质修饰硫 (IV) 化学的最新进展.
- 突出这些新策略在各种应用中的潜力,包括近距离标签和药物输送.
主要方法:
- 基于硫的试剂设计中的协同创新.
- 反应中间体的调制.
- 生物对等反应的开发,用于选择性修饰.
主要成果:
- 建立具有选址性,条件响应性和功能性救援能力的多功能修改工具箱.
- 证明硫化学作为生物分子后期功能化的强大平台.
结论:
- 硫 (IV) 化学为现有的和蛋白质修饰方法提供了一个有前途的替代方案.
- 这些进步为未来在化学生物学和治疗干预中的应用带来了巨大的潜力.
相关概念视频
Protein Modifications in the RER
4.9K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
4.9K
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids
129
Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme...
129
Covalently Linked Protein Regulators
6.7K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.7K
Protein Folding
7.5K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
7.5K
Peptide Bonds
71.4K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
71.4K
Preparation and Reactions of Sulfides
4.7K
Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
4.7K

