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相关概念视频

Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Protein-Protein Interfaces02:04

Protein-Protein Interfaces

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Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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通过使用计算机辅助设计修改蛋白界面来预测IL-18/IL-18R结合的改善.

Napat Prompat1,2, Chariya Peeyatu1, Jirakrit Saetang3

  • 1Department of Biomedical Sciences and Biomedical Engineering, Faculty of Medicine, Prince of Songkla University, Songkhla 90110, Thailand.

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概括

使用计算方法来设计突变,以增强用于癌症免疫治疗的INTERLEUKIN-18 (IL-18) 活性. 这些设计突变显示出改善IL-18的潜力.

关键词:
细胞因子介导的免疫疗法.介质蛋白-18的使用方法分子动力学模拟模拟结构导向设计是指导设计.

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科学领域:

  • 生物化学和分子生物学
  • 免疫学 免疫学 免疫学
  • 计算生物学 计算生物学

背景情况:

  • 细胞因子免疫疗法,特别是使用INTERLEUKIN-18 (IL-18) 是一个有前途的癌症治疗策略.
  • IL-18通过增强自然杀手 (NK) 和细胞毒性T细胞活性来增强抗瘤反应.
  • 优化IL-18与其受体的相互作用是提高其治疗功效的关键.

研究的目的:

  • 通过计算设计和预测增加IL-18生物活性的突变.
  • 研究特定突变对IL-18受体结合和稳定性的影响.
  • 探索计算机辅助设计方法,以开发更强大的基于IL-18的癌症疗法.

主要方法:

  • 基于结构的计算能量计算被用来识别潜在的突变.
  • 用分子动力学 (MD) 模拟来评估突变IL-18.的稳定性和形状变化.
  • 分析的重点是关键蛋白质区域的静电相互作用和灵活性.

主要成果:

  • 预计四种候选突变 (E6M,E6M+N111S+R131G,E6M+K129M+R131G,E6M+N111S+K129M+R131G) 可以增强IL-18受体的结合和稳定性.
  • MD模拟表明,突变不会影响蛋白质的整体稳定性,但会增加β8-β9毛环的灵活性.
  • 突变IL-18的动态行为表明了改善生物活动的潜力.

结论:

  • 计算机辅助设计是提高IL-18细胞因子功能的有效策略.
  • 鉴定的突变为开发用于癌症免疫治疗的改进IL-18变体提供了基础.
  • 需要对整个IL-18受体综合体进行进一步的模拟,以充分验证这些发现.