関連する実験動画
Updated: Mar 29, 2026

07:11
Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
3.2K
ブテラゼ1:ペプチドとタンパク質のマクロサイクリングのための多用途リガゼ
Giang K T Nguyen1, Antony Kam1, Shining Loo1
1School of Biological Sciences, Nanyang Technological University , 60 Nanyang Drive, Singapore.
Journal of the American Chemical Society
|December 4, 2015
まとめ
ブテラゼ1を用いた新しい方法は,ペプチドとタンパク質を急速にマクロサイクライズします. この効率的なタンパク質サイクリング技術は 現在の方法より2万倍速く 数分で高い収穫量を得ることができます
科学分野:
- 生物化学
- 分子生物学
- 薬物の発見
背景:
- マクロサイクリングは新しい薬や タンパク質の設計に不可欠です
- マクロサイクル合成の既存の方法は,一般的に適用可能で効率的でないことが多い.
研究 の 目的:
- ペプチドとタンパク質のマクロサイクリングのための高効率で一般的な方法を開発する.
- 新しい方法の効率を既存のタンパク質サイクリング技術と比較する.
主な方法:
- タンパク質とペプチドのマクロサイクリングにブテラゼ1を用いる.
- タンパク質の大きさの範囲 (26 ~ > 200 残基) でテストした.
主要な成果:
- ペプチドとタンパク質の高効率のマクロサイクリングを達成した.
- ソルターゼA媒介サイクリングより2万倍速い反応率を示した.
- 反応は数分で完了し,最大95%の収量が得られる.
結論:
- ブテラゼ1は,タンパク質とペプチドのマクロサイクリングに著しく速く効率的なアプローチを提供します.
- この方法は,薬剤設計とタンパク質工学の応用のための貴重な新しいツールを提供します.
- ブテラゼ1の速度と効率は,現在のタンパク質サイクリング戦略の限界を克服します.
関連する概念動画
Peptide Bonds
86.5K
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...
86.5K
Ligand Binding and Linkage
6.0K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
6.0K
Bacterial Protein Maturation
701
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...
701
The Proteasome
2.0K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
2.0K
Protein Folding
12.5K
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...
12.5K

