机械激活的粉网状纳米结构将酸作为结构和功能载荷的陷
Siyu Yao1, Haohao Hu1,2, Yushi Li1
1College of Biosystems Engineering and Food Science, National-Local Joint Engineering Research Center of Intelligent Food Technology and Equipment, Zhejiang Key Laboratory of Agro-food Resources and High-value Utilization, Zhejiang International Scientific and Technological Cooperation Base of Health Food Manufacturing and Quality Control, Zhejiang University, Hangzhou 310058, China.
Biomacromolecules
|May 12, 2025
概括
这项研究开发了一种新的粉纳米结构,可以使用化方法有效加载酸 (FA). 这种绿色方法显著提高了多含量,并为各种应用提供了酶耐药性.
科学领域:
- 材料科学 材料科学 材料科学
- 聚合物化学 聚合物化学
- 生物化学 生化学
背景情况:
- 聚烯聚合物复合材料正在获得可扩展应用的关注.
- 粉聚合物通常通过没有催化剂的非共价相互作用来表现出低载荷的疏水性多.
研究的目的:
- 开发一种网状粉纳米结构,用于增强多 (酸) 载荷.
- 为多复合网络建立一种无催化剂的绿色合成路径.
主要方法:
- 从一种粉纳米球前体 (preSNS) 来定制一个网状粉纳米结构,通过化捕获酸 (FA).
- 使用动态高压微流体化激活前SNS-FA网络.
- 使用SEM,FTIR,XRD,NMR (13C,1H),XPS和分子动力学模拟进行表征.
主要成果:
- 与传统粉相比,在SNS-FA前的网络中达到异常高的FA含量 (∼38.0%) (∼1.5%).
- 通过全面的表征和模拟,确认了结构变化和新的结模式 (-COOR-).
- 证明了SNS-FA前网络的显著酶性水解耐药性 (高达83.8%).
结论:
- 建立了一种高性能,无催化剂的合成路径,用于化多复合网络.
- 开发的纳米结构显示了营养递送,食品包装和农业的潜力.
相关概念视频
Acid Strength and Molecular Structure
Binary Acids and Bases
In the absence of any leveling effect, the acid strength of binary compounds of hydrogen with nonmetals (A) increases as the H-A bond strength decreases down a group in the periodic table. For group 17, the order of increasing acidity is HF < HCl < HBr < HI. Likewise, for group 16, the order of increasing acid strength is H2O < H2S < H2Se < H2Te. Across a row in the periodic table, the acid strength of binary hydrogen compounds increases with increasing...
In the absence of any leveling effect, the acid strength of binary compounds of hydrogen with nonmetals (A) increases as the H-A bond strength decreases down a group in the periodic table. For group 17, the order of increasing acidity is HF < HCl < HBr < HI. Likewise, for group 16, the order of increasing acid strength is H2O < H2S < H2Se < H2Te. Across a row in the periodic table, the acid strength of binary hydrogen compounds increases with increasing...
Assembly of Cytoskeletal Filaments
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...
Generation of Straight or Branched Actin Filaments
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Formation of Higher-order Actin Filaments
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 networks...
The high-order actin networks...
What are Proteins?
Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight. Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional structure...
Mechanical Protein Function
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.


