氨基酸纳米球的超分子组装成双折断的微丝带
Chang Du1, Giuseppe Falini, Simona Fermani
1Center for Craniofacial Molecular Biology, School of Dentistry, University of Southern California, 2250 Alcazar Street, CSA 103, Los Angeles, CA 90033, USA.
概括
氨基酸蛋白自组装成纳米球,形成微丝带,指导碳酸酸盐晶体的生长. 这一发现提供了关于牙面膜生物矿物化和面向晶体形成的见解.
科学领域:
- 生物矿物化的研究研究.
- 材料科学是一种材料科学.
- 蛋白质自我组装的过程
背景情况:
- 牙面膜和骨头共享碳酸阿帕提特晶体组成.
- 乳独特的是缺乏原蛋白,并且不会重塑.
- 氨基原蛋白纳米球的自我组装对于质晶体的生长至关重要.
研究的目的:
- 为了研究在体外的结构的形成从 amelogenin纳米圈自组装.
- 阐明 amelogenin 在控制 apatite 晶体方向方面的作用.
主要方法:
- 在体外通过 amelogenin nanosphere 超分子组装形成微带结构.
- 微带衍射模式的分析以确定结构周期性.
- 通过这些结构促进的 in vitro apatite 晶体生长的观察.
主要成果:
- 在试验室中成功形成了双断裂的微带结构.
- 衍射模式证实了微带内的周期性晶体单位.
- 阿帕提特晶体沿着c轴成长,与微带长轴平行.
- 纳米球的中间线性阵列为阿梅洛金因的作用提供了证据.
结论:
- 氨基原蛋白纳米圈自组装可以产生有序的微带结构.
- 这些微丝带有助于碳酸阿帕晶体的定向生长.
- 这些发现增强了对阿梅洛金因在牙面膜生物矿物化中的作用的理解.
相关概念视频
Protein Folding
Overview
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...
A protein's shape is critical to its function. For example, an enzyme can...
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...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
The Structure of Intermediate Filaments
The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm). These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...
Intermediate filaments...
Formation of Intermediate Filaments
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.
Fibrous Proteins
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...


