通过分子动力学模拟研究的纤维素与zwitterionic peptoid刷的特定和非特异性相互作用
David L Cheung1, Phillip B Messersmith2,3,4, King Hang Aaron Lau5
1School of Biological and Chemical Sciences, University of Galway, Galway, Ireland. david.cheung@universityofgalway.ie.
Physical chemistry chemical physics : PCCP
|November 13, 2025
概括
兹维特里奥尼克类刷子对抗污垢表面的表现非常有希望. 分子动力学模拟揭示了特定的蛋白质相互作用,指导了可控制细胞附着和蛋白质结合的表面设计.
科学领域:
- 生物材料科学 生物材料科学
- 表面化学 表面化学
- 计算生物物理学的计算生物物理学
背景情况:
- 采用Zwitterionic聚合物刷,以防止表面上的非特异性蛋白质相互作用.
- 类仿真类提供序列特定的平台,用于防刷和蛋白质结合基因.
- 对蛋白质-类相互作用的分子层次理解是有限的.
研究的目的:
- 用原子分子动力学 (MD) 模拟来分析纤维素蛋白III型 (FnIII) 9和10域与zwitterionic peptoid刷之间的相互作用.
- 为了比较这些相互作用与聚沙科辛的相互作用,一个无电荷的peptoid.
- 获得对蛋白质-类相互作用的分子洞察力,并为先进生物材料的设计提供信息.
主要方法:
- 用原子分子动力学 (MD) 模拟来研究蛋白质-类相互作用.
- 模拟分析了纤维素蛋白III型 (FnIII) 9和10域与zwitterionic类刷子和聚沙科辛的相互作用.
- 实验性蛋白质吸附数据指导了模拟类链密度的选择.
主要成果:
- 模拟结果与各种链密度的实验蛋白质吸附趋势保持一致.
- 确定了特定的FnIII9-10区域和氨基酸,这些氨基酸与聚沙可素和zwitterionicpeptoids的相互作用有关.
- 观察到与zwitterionic peptoid设计的更强的相互作用,与蛋白质整合素结合动机的方向远离表面.
结论:
- 这项研究为蛋白质-类相互作用提供了新的分子洞察力.
- 兹维特里奥尼克类刷子显示出增强抗性质和受控蛋白质相互作用的潜力.
- 这些发现表明,有可能设计特定的类序列,以呈现细胞结合动机并介导细胞附着.
相关概念视频
01:25Fibronectins Connect Cells with ECM
3.3K
Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
3.3K
02:04Protein-protein Interfaces
14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K
02:35Noncovalent Attractions in Biomolecules
63.0K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
63.0K
01:56Structural Protein Function
29.7K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
29.7K