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関連する概念動画

Protein Folding01:25

Protein Folding

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 Folding01:22

Protein Folding

Overview
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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関連する実験動画

Updated: Jun 27, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

ペプチドデンドリマー内のアルファヘリックス安定化.

Sacha Javor1, Antonino Natalello, Silvia Maria Doglia

  • 1Department of Chemistry and Biochemistry, University of Berne, Freiestrasse 3, CH-3012 Berne, Switzerland.

Journal of the American Chemical Society
|December 5, 2008
PubMed
まとめ

この研究では,特定のアルファヘリル型ペプチドデンドリマーが,線形ペプチドよりも安定していることが示されています. この発見は,天然のアミノ酸を使用してタンパク質のような構造を作り出すための新しい可能性を提供します.

科学分野:

  • バイオケミストリー バイオケミストリー
  • ポリマー化学のポリマー化学について
  • 構造生物学 構造生物学とは

背景:

  • ペプチド dendrimersは,様々な分野で潜在的なアプリケーションを持つ分岐分子です.
  • デンドリマーの構造的安定性を理解することは,その設計と機能にとって極めて重要です.
  • 線形ペプチドは,環境ストレス下での展開と集積に敏感です.

研究 の 目的:

  • 第2世代のアルファヘリル型ペプチドデンドリマーとその線形同位体の安定性を比較する.
  • デンドリマーにおける安定性を高める構造的基礎を調査する.
  • タンパク質の安定したアナログとしてのデンドリマーの可能性を調査する.

主な方法:

  • アルファヘリカルペプチドデンドリマーと線形ペプチドの合成と特徴付け.
  • pH誘発による展開の評価.
  • 温度によって引き起こされる分子間結合の評価.

主要な成果:

  • アルファヘリル型ペプチド・デンドリメアは,線形ペプチドと比較して,pH誘発による展開に対して著しく高い安定性を示した.
  • デンドリマーはまた,温度によって誘発される分子間結合に対する耐性が向上したことを示した.

さらに関連する動画

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

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

Published on: November 21, 2013

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

関連する実験動画

Last Updated: Jun 27, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

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

Published on: November 21, 2013

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

  • 提案されたメカニズムは,連続した分岐点を横断するアルファヘリックスを含み,安定性を与えます.
  • 結論:

    • 研究されたペプチドデンドリマーは,そのユニークなアルファヘリル構造により,前例のない安定性を示しています.
    • この研究は,天然のアミノ酸のみを使用してタンパク質を模倣する折りたたまれたデンドリート構造を設計するための道を切り開きます.
    • この発見は,新しい生体材料と治療薬の開発に意味を持つ.