用氨基酸功能化的金纳米粒子对α-chymotrypsin进行可调节的抑制和变性
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Updated: Aug 14, 2026

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Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
Chang-Cheng You1, Mrinmoy De, Gang Han
1Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.
Journal of the American Chemical Society
|September 15, 2005
概括
与氨基酸功能化的金纳米粒子被研究为蛋白质结合. 氨基酸特性影响结合亲和力和蛋白质稳定性,影响纳米粒子-蛋白质相互作用.
科学领域:
- 生物技术是生物技术.
- 纳米技术 纳米技术
- 生物化学 生物化学
背景情况:
- 黄金纳米颗粒 (AuNPs) 广泛用于生物医学应用.
- 控制纳米粒子表面特性对于特定的生物分子相互作用至关重要.
研究的目的:
- 调查l-氨基酸终端在黄金纳米粒子表面对蛋白质结合的影响.
- 了解静电和疏水相互作用在纳米粒子-蛋白质复合体形成中的作用.
主要方法:
- 制造具有多种l-氨基酸终端的水溶性黄金纳米粒子.
- 通过活性测定,凝电泳,泽塔电位,圆形二极化和光光谱学来研究α-chymotrypsin (ChT) 相互作用.
主要成果:
- 对于受体-蛋白系统的结合常数在10(6) 到10(7) M(-1).
- 蛋白质结合能力取决于纳米粒子表面积和电荷密度.
- 水友性氨基酸侧链破坏了ChT结构的稳定性,而疏水性氨基酸则表现出较慢的变性.
- 观察到氨基酸水性,结合亲和力和变性率之间存在相关性.
结论:
- 纳米粒子表面化学,特别是氨基酸终端,显著影响蛋白质结合和稳定性.
- 电静电和水相互作用都是纳米粒子-蛋白质复合体形成的关键驱动因素.
- 氨基酸侧链特性决定了蛋白质在与功能化纳米颗粒结合时的变性程度.
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Enzyme Inhibition
Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
Protein Denaturation
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

