Aza-Glycineはコラーゲンの高安定性を誘導する
Yitao Zhang1, Roy M Malamakal1, 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
|September 15, 2015
まとめ
合成化学者はグリシンをアザグリシンに置き換え コラーゲンを改造しました この置換により水素結合が強化され,超安定したトリプルヘリックスが形成され,新しいバイオ分子工学のアプローチが示されました.
科学分野:
- 生物化学
- ポリマー化学
- 合成生物学
背景:
- 水素結合は生物分子の相互作用と 核酸のような天然のバイオポリマーの安定性にとって不可欠です
- 自然なバイオポリマーはしばしば最大化された水素結合を示し,ネイティブの改変によってさらなる安定化を制限する.
- グリシンは,現在,コラーゲン構造内の置換に耐受性がないと考えられている唯一のアミノ酸です.
研究 の 目的:
- バイオポリマーの水素結合を強化するための合成改変の可能性を調査する.
- コラーゲンのトリプルヘリックス安定性に対するアザ-グリシンによるグリシン置換の効果を調査する.
- 高度なバイオポリマーシステムでハイパー安定性を達成する方法を実証する.
主な方法:
- 合成化学を使って コラーゲンペプチドを作りました
- コラーゲン配列内の特定の位置にアザグリシンを導入した.
- 生体物理的技術を用いて,結果として生じる三重螺旋コラーゲンの構造と安定性の変化を分析した.
主要な成果:
- グリシンをアザグリシンに置き換えることで,交差点の交叉鎖の水素結合の数が増加しました.
- 修正されたコラーゲンは 三重ヘリキルの形状で安定性が向上し,この現象はハイパー安定性と呼ばれています.
- この改変は 自然の構成要素を最小限に 妨害する代替手段を用いて行われました
結論:
- バイオポリマーシステムにおける水素結合の最大化は,合成改変によって効果的に達成できます.
- アザグリシン置換は,コラーゲンおよび潜在的に他のバイオポリマーの安定性を高めるための実行可能な戦略です.
- この研究は,構造的整合性と機能を向上した新しいバイオマテリアルを設計するための道を開きます.
関連する概念動画
Fibril-associated Collagen
3.6K
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...
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...
3.6K
Type IV Collagen of Basal Lamina
3.4K
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...
A type IV collagen molecule has six alpha chains which can...
3.4K
Structural Protein Function
30.5K
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...
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...
30.5K
Glycosaminoglycans
7.7K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
7.7K
Collagens are the Major Structural Proteins of ECM
6.3K
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...
Connective tissue proper includes loose...
6.3K


