来自Agaricus bisporus的Hydrophobin I类组装产生了不同的粉样纤维
Jesús Rojas-Osnaya1, Hugo Nájera1
1Universidad Autónoma Metropolitana-Cuajimalpa. Departamento de Ciencias Naturales. Laboratorio de Biofisicoquímica, Av. Vasco de Quiroga 4871. Col. Santa Fe Cuajimalpa, Alcaldía Cuajimalpa, Mexico City, CP 05348, Mexico.
Biochimica et biophysica acta. Proteins and proteomics
|September 28, 2024
概括
这项研究净化了Agaricus bisporus水类I (ABH4) 的水,揭示了其结构性质和自我组装成粉样纤维. ABH4 影响表面特性,纤维的形成是依赖pH的.
科学领域:
- 生物化学 生物化学
- 蛋白质科学 蛋白质科学
- 材料科学 材料科学 材料科学
背景情况:
- 水蛋白是两性蛋白质,以其在生物系统中的作用而闻名.
- 了解水蛋白的结构功能关系对于生物技术应用至关重要.
研究的目的:
- 从Agaricus bisporus (ABH4) 中提取,净化和表征一级水素.
- 在各种条件下研究ABH4的自组装特性和结构变化.
主要方法:
- 使用SDS-PAGE提取和净化蛋白质.
- 蛋白质结构预测和分析 (循环二元化).
- 表面性能分析 (接触角度测量).
- 纤维细胞形成研究 (ThT测定,SEM,AFM).
主要成果:
- 有效提取和净化ABH4 (12 kDa) 含有八种囊残留物.
- ABH4改变了Teflon和玻璃的表面接触角度,其临界粒度为221μg/mL.
- 纤维细胞的形成在酸性/中性pH值处是有利的,在基本pH值处是抑制的;合体Teflon会影响纤维细胞的产生.
- 旋转诱导二次结构变化 (增加阿尔法螺旋和β片含量).
- SEM和AFM揭示了ABH4在玻璃和上形成的粉样结构.
结论:
- ABH4具有独特的结构和自组装特性.
- 环境因素,如pH值显著影响ABH4纤维素的形成.
- 这项研究提供了对水类I组装和潜在应用的见解.
相关概念视频
Amyloid Fibrils
9.3K
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,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.3K
Formation of Higher-order Actin Filaments
3.0K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
The high-order actin...
3.0K
Assembly of Cytoskeletal Filaments
18.6K
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...
18.6K
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
Mechanism of Filopodia Formation
2.3K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.3K
Formation of Intermediate Filaments
2.9K
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...
2.9K


