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関連する概念動画

Fibril-associated Collagen01:11

Fibril-associated Collagen

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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

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Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
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Collagens are the Major Structural Proteins of ECM01:13

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Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
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Structural Protein Function01:56

Structural Protein Function

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
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Protein Folding01:22

Protein Folding

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Overview
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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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Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
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Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

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トリプルヘリコラーコラーゲンの安定化のための一般的ソリューション

Yitao Zhang1, Madison Herling1, David M Chenoweth1

  • 1Department of Chemistry, University of Pennsylvania , 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, United States.

Journal of the American Chemical Society
|July 14, 2016
PubMed
まとめ
この要約は機械生成です。

コラーゲンペプチドのグリシンをアザグリシンに置き換えると,追加の水素結合によって安定性と自己組み立てが強化されます. この戦略は,設計されたペプチド材料を最適化し,コラーゲントリプルヘリクスを安定させます.

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Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment
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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

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関連する実験動画

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科学分野:

  • 生物化学
  • 材料科学
  • 構造生物学

背景:

  • 水素結合は バイオ分子構造と安定性にとって 極めて重要です
  • 自然のタンパク質の構成要素は 水素結合に依存しているため 限界があります
  • コラーゲンの構造は水素結合によって安定し,グリシンが保存された残基である.

研究 の 目的:

  • コラーゲンペプチドにおけるアザ-グリシンによるグリシン代用の影響を調査する.
  • コラーゲンペプチドの安定性や自己組織化への影響を調査する.
  • コラーゲンのトリプルヘリクスを安定させ,ペプチド材料を設計するための新しい戦略を開発する.

主な方法:

  • アザグリシン置換によるコラーゲンペプチドの合成
  • ペプチドの安定性と自己組み立ての性質の分析
  • アザグリシンによる構造変化の特徴

主要な成果:

  • アザグリシン置換は,コラーゲンペプチドの安定性と自己組み立てを著しく強化します.
  • アザグリシンでグリシン残基を完全に置き換えることができます.
  • 最小の自己組み立てコラーゲンペプチドシステムが達成されました.
  • 溶解した接点における水素結合の重要性を示した.

結論:

  • アザグリシンは,コラーゲンの安定性を改善する追加の水素結合ドナーを提供します.
  • 設計されたペプチド材料を最適化するための新しい戦略を提供します.
  • コラーゲントリプルヘリクスの安定化のための一般的な溶液が特定されました.