在疏水表面上组装阿尔法螺旋涂层
Joanna R Long1, Nathan Oyler, Gary P Drobny
1Department of Bioengineering, University of Washington, Seattle, Washington 98195, USA.
Journal of the American Chemical Society
|May 30, 2002
概括
研究人员使用固态NMR研究了对聚合物表面的吸附. 他们发现,短,结构化的可以不可逆地吸附,为生物相容性表面修饰提供了洞察力.
科学领域:
- 生物材料科学 生物材料科学
- 聚合物化学 聚合物化学
- 生物物理学的生物物理.
背景情况:
- 提高生物材料的生物相容性往往需要将生物分子固定在表面上.
- 验证固定生物分子的结构和动态对于理解它们的功能至关重要.
- 目前用于表面修改和验证的方法在复杂的环境中存在挑战.
研究的目的:
- 在多孔疏水性聚合物表面研究设计的吸附和结构完整性.
- 确定稳定,结构化吸附所需的最小长度和条件.
- 证明固态核磁共振 (NMR) 技术的实用性,用于表征固定.
主要方法:
- 小型线性的合成与交替的氨酸和氨酸残留物.
- 在水溶液中的多孔聚烯表面上进行吸附研究.
- 应用传统和先进的固态NMR技术,包括二维双量子实验.
- 分析体结构,动态和吸附作为螺旋长度和序列周期性的函数.
主要成果:
- 在聚乙烯表面吸附的酸采用了稳定的螺旋式二次结构.
- 在NMR时间尺度上没有大振幅动态,这表明不可逆向的吸附.
- 即使是短的 (七种氨基酸) 也可以在更高的度下与定义的结构吸附.
- 固态核磁共振,特别是二维双量子方法,在异质聚合物系统中提供了高分辨率的结构数据.
结论:
- 结构性可以有效地吸附到聚合物表面,从而可能提高生物相容性.
- 固态NMR是一种强大的工具,用于阐明复杂材料中固定生物分子的结构和动态.
- 这些发现为设计具有量身定制的生物分子相互作用的表面改性聚合物材料提供了基础.
相关概念视频
Protein Organization
Overview
Protein Folding
Overview
Peptide Bonds
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
Coat Assembly and GTPases
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...
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...
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.
The primary structure of a protein is its amino acid sequence.
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 Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...


