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相关概念视频

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:
14.8K
Conserved Binding Sites01:49

Conserved Binding Sites

5.0K
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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Protein-protein Interfaces02:04

Protein-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

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相关实验视频

Updated: Jan 11, 2026

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates
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Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

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评估BindCraft用于高亲和性的生成设计.

Mike Filius1,2, Thanasis Patsos1,2, Hugo Minnee1,2

  • 1Leiden Academic Center for Drug Research, Leiden University, Leiden 2333 CC, The Netherlands.

ACS chemical biology
|November 18, 2025
PubMed
概括
此摘要是机器生成的。

BindCraft是一个生成人工智能平台,通过分析蛋白质结构,成功地设计了用于药物发现的高 afinity . 这种方法对开发针对MDM2和WDR5.5等标的新疗法充满希望.

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A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
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A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

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相关实验视频

Last Updated: Jan 11, 2026

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates
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Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

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A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
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A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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科学领域:

  • 计算生物学是一种计算生物学.
  • 药物发现 药物发现
  • 蛋白质工程是一种蛋白质工程.

背景情况:

  • 从蛋白质结构中开发高亲缘关系联体至关重要,但具有挑战性.
  • 短具有治疗潜力,但由于缺乏稳定的结构,新的功能性的产生是困难的.

研究的目的:

  • 评估BindCraft,一个结构导向的生成建模平台,用于新的体设计和高亲和度联体发现.
  • 评估BindCraft产生的功能性的能力,仅基于目标蛋白质结构.

主要方法:

  • 利用BindCraft,一个结构引导的生成AI平台,用于新的体设计.
  • 合成并经过实验验证的产生的酸对抗瘤学点MDM2和WDR5.5.
  • 采用竞争分析和亲和度测量 (KD) 来确认结合特异性和强度.

主要成果:

  • BindCraft为MDM2产生了70种独特的;15种合成中的7种显示了纳米分子亲和力和特定位点的结合.
  • 在9种为WDR5设计的中,有6种与MYC结合部位的亚微分子亲和力结合.
  • 使用BindCraft预测的类优化提高了WDR5绑定器功效的6倍,达到39nM的KD.

结论:

  • BindCraft在产生针对特定蛋白质标的高亲和方面取得了显著的成功,与传统显示技术相竞争.
  • 该平台显示了加速开发基于的治疗方法的潜力.
  • 需要进一步评估,因为BindCraft在本研究中没有为PD-1和PD-L1目标产生结合剂.