四重堆積相互作用によって誘発される分子図形8ノードの自己組み立て
Li-Long Dang1, Hui-Jun Feng1, Yue-Jian Lin1
1Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, State Key Laboratory of Molecular Engineering of Polymers, Department of Chemistry, Fudan University, Shanghai 200433, P. R. China.
Journal of the American Chemical Society
|October 2, 2020
まとめ
研究者は,希少な分子形8ノット (41) を効率的に合成するための四重のスタッキング戦略を開発しました. この方法は,NDIベースのリガンドとCp*Rh単位を使用して,ノードの安定性と可逆変換を制御できます.
科学分野:
- 超分子化学
- 有機合成
- 材料科学
背景:
- 分子結び目,特にフィギュア8の結び目 (41) は,複雑な絡み合いのために合成的に困難です.
- 既存のノード合成方法はしばしば非効率で,複数のステップが必要です.
研究 の 目的:
- 分子形8ノードの合成のための効率的で信頼性の高い方法を開発する.
- これらの複雑な分子構造の安定性と構造変化に影響を与える要因を調査する.
主な方法:
- ナフタレンジイミド (NDI) ベースのピリジルリガンドとCp*Rhの構成要素を組み合わせた4つのスタッキング戦略が採用されました.
- 単一のステップでセルフアセンブリを使用し,望ましいフィギュア8ノット構造を形成しました.
- 構造の特徴と確認のために,X線結晶学とNMRスペクトロスコーピーを用いた.
主要な成果:
- 分子形8ノット (41) の効率的な自己組み立ては,四重のスタッキング相互作用によって達成された.
- メタノールで合成されたノードの安定性は,Cp*Rh単位のサイズに敏感であることが判明した.
- 濃度と外部の刺激 (溶媒,ゲスト) によって引き起こされる,フィギュア8ノットとメタロレクトアングルの間の可逆的な構造変化が観察されました.
結論:
- 複合的な分子構造の 効率的な経路を提示します
- この研究は,これらの超分子システムにおける調整可能な安定性と動的構造的行動を示しています.
- この研究は,制御可能な性質を持つ新しいトポロジカル分子構造を設計するための基礎を提供します.
関連する概念動画
Assembly of Cytoskeletal Filaments
26.0K
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...
26.0K
Formation of Intermediate Filaments
3.6K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
3.6K
Disassembly of Intermediate Filaments
2.5K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.5K
Formation of Higher-order Actin Filaments
3.4K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
The high-order actin...
3.4K
Generation of Straight or Branched Actin Filaments
3.5K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.5K
Protein Folding
125.2K
Overview
125.2K


