金属促进的高阶组装的二硫化物叠加螺旋式桶
Ashutosh Agrahari1, Mark Lipton1, Jean Chmielewski1
1Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47907, USA.
Nanomaterials (Basel, Switzerland)
|October 14, 2023
概括
研究人员创建了基于的螺旋式桶,可以自组装成3D矩阵. 这些生物材料可以容纳货物,显示生物技术在细胞和组织生长中的应用潜力.
科学领域:
- 生物材料科学 生物材料科学
- 超分子化学 超分子化学
- 蛋白质工程是指蛋白质工程.
背景情况:
- 基于的螺旋式桶为货物托管提供了疏水性腔.
- 分层组装是先进生物材料设计的关键.
研究的目的:
- 用金属离子连接剂合成二硫化物合螺旋.
- 为了研究这些桶的自组装成更高阶结构.
- 探索这些生物材料在生物技术中的潜力.
主要方法:
- 来自两性的二硫化物合螺旋式桶的合成.
- 在形结构优化形螺旋桶 (5HB1).
- 金属离子促进的自组装成3D矩阵.
- 用疏水性染料和His标记蛋白质对矩阵进行装饰.
主要成果:
- 一个单步反应从16种氨基酸中产生了一个稳定的形形桶 (5HB1).
- 在分析中,在5HB1结构中发现了~6 Å的疏水腔.
- 金属离子介导的组件形成了一个3D矩阵,具有可调节的装饰功能.
- 该矩阵成功地结合了疏水性染料和HIS标记的蛋白质.
结论:
- 用二硫化物合的螺旋式桶作为分层组装的多功能构建块.
- 由此产生的3D基可以封装各种分子和蛋白质.
- 这种基于的生物材料显示出生物技术的巨大潜力,包括用于细胞和组织生长的受控释放应用.
相关概念视频
Protein Folding
118.3K
Overview
118.3K
Protein Complex Assembly
10.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.6K
Assembly of Cytoskeletal Filaments
20.9K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
20.9K
Multi-pass Transmembrane Proteins and β-barrels
5.3K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.3K
Formation of Intermediate Filaments
3.1K
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...
3.1K
Porin Insertion in the Outer Mitochondrial Membrane
3.0K
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
3.0K


