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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Protein Folding01:25

Protein Folding

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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...
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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ペプチドアンフィフィールアセンブリにおける経路選択

Peter A Korevaar1, Christina J Newcomb, E W Meijer

  • 1Institute for Complex Molecular Systems and Laboratory of Macromolecular and Organic Chemistry, Eindhoven University of Technology , 5600 MB Eindhoven, The Netherlands.

Journal of the American Chemical Society
|June 10, 2014
PubMed
まとめ

ペプチドアンフィフィルの様々な製法により,異なる超分子構造が形成されます. ベータシートへの組み立ては,ヘクサフッロアイソプロパノール (HFIP) のような溶媒によって遅らせられるが,安定したフィラメントを形成する.

科学分野:

  • 超分子化学 超分子化学
  • マテリアルサイエンス 材料科学
  • バイオフィジックス 生物物理学

背景:

  • 超分子化学は構造形成を研究しているが,組み立て経路は十分に研究されていない.
  • ペプチドアンフィフィルは,環境条件に基づいて様々な構造に自己組織化します.
  • アセンブリダイナミクスの理解は,超分子形態の制御に不可欠です.

研究 の 目的:

  • 異なる製剤プロトコルがペプチドアンフィファイルの自己組み立てにどのように影響するか調査する.
  • ペプチドアンフィフィール組立に対する溶媒,特にヘクサフッロアイソプロパノール (HFIP) の効果を測定する.
  • 結果となる超分子構造の形態学と運動的安定性を特徴付ける.

主な方法:

  • HFIPの濃度が異なる水溶液中のペプチドアンフィフィルの自己組み立て.
  • 二次構造に敏感な技術 (例えば,スペクトロスコーピー,顕微鏡) を用いた形態学的特徴づけ.
  • 組み立てと分解のプロセスの運動分析.

主要な成果:

  • 異なる調製プロトコルにより,異なる超分子形態が得られました:ベータシートを持つ長い繊維と,ランダムなコイル形状を持つより小さな集積物.
  • ベータシートへの組み立て率は,HFIP濃度が増加するにつれて低下し,一時的な溶液条件の影響を受けた.

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  • ベータシートフィラメントの自発的な核形成のために,HFIPの重要な分数 (21パーセント以下) が特定されました.
  • 形成されたベータシートアセンブリは,高い運動安定性と緩やかな分解性を示した.

    • 結論:

    • 製剤経路はペプチドアンフィフィルの超分子形態学に著しく影響する.
    • HFIPは不安定化溶媒として作用し,βシート形成運動を調節する.
    • この研究は,超分子構造と安定性を制御する際に組み立てダイナミクスの重要性を強調しています.
    • アセンブリダイナミクスに関する洞察は,特定の機能アプリケーションのための経路を最適化するための経路を提供します.