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相关概念视频

Enzyme Inhibition01:30

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.
Oral Hypoglycemic Agents: α-Glucosidase Inhibitors01:19

Oral Hypoglycemic Agents: α-Glucosidase Inhibitors

α-glucosidase inhibitors, including acarbose (Precose), miglitol (Glyset), and voglibose (Voglib) (primarily available in Asia), are drugs that control blood sugar levels by delaying the digestion of starch and disaccharides. They achieve this by inhibiting α-glucosidase enzymes in the intestine, which slow the absorption of carbohydrates in the intestine, which in turn leads to a prolonged release of the glucoregulatory hormone GLP-1 from intestinal L-cells.
Acarbose and miglitol are typically...
Dipeptidyl Peptidase 4 Inhibitors01:23

Dipeptidyl Peptidase 4 Inhibitors

Dipeptidyl peptidase 4 (DPP-4) is a serine protease widely distributed in the body. It's involved in the inactivation of GLP-1 and GIP hormones, which are crucial for insulin regulation. DPP-4 inhibitors, such as sitagliptin (Januvia), saxagliptin (Onglyza), linagliptin (Tradjenta), alogliptin (Nesina), and vildagliptin (Galvus), help increase the proportion of active GLP-1, enhancing insulin secretion. These inhibitors work by competitively binding to DPP-4. This binding causes a significant...

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相关实验视频

Updated: Jul 17, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

糖酶抑制:对18种假定的过渡状态模仿剂的结合的评估.

Tracey M Gloster1, Peter Meloncelli, Robert V Stick

  • 1York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, UK.

Journal of the American Chemical Society
|February 7, 2007
PubMed
概括

设计酶抑制剂是新药的关键. 这项研究分析了Thermotoga海洋家族1β-葡萄糖酶 (TmGH1) 的18种过渡状态模仿抑制剂,发现溶解效应显著影响结合热力学.

科学领域:

  • 生物化学 生物化学
  • 酶动力学 酶动力学
  • 药物发现 药物发现

背景情况:

  • 糖酸酶抑制剂对于理解酶机制和开发治疗癌症,艾滋病毒,流感和糖尿病等疾病的疗法至关重要.
  • 设计强效抑制剂依赖于酶对它们的过渡状态的高度亲和力.
  • 之前的研究表明,糖酶抑制剂的抑制模式令人困惑.

研究的目的:

  • 为了分析18种过渡状态模仿抑制剂与Thermotoga海洋家族1β-葡萄糖酶 (TmGH1) 酶的结合.
  • 建立一个抑制概况,阐明控制连接体结合的因素.
  • 通过协同方法研究抑制剂结合的热力学基础.

主要方法:

  • 确定了酶活性和抑制的pH依赖.
  • 抑制剂-酶复合体的溶解X射线晶体结构高达1.65 Å的分辨率.
  • 使用异热定位热量计,以获得结合的热力学特征.

主要成果:

  • 描述了18种假定的过渡状态模仿抑制剂.
  • 观察到抑制剂化学和热力学解剖热力学之间的相关性很小.
  • 在抑制剂组合中表现出强烈的力-力补偿.

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A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors
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Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
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A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors
10:28

A Semi-High-Throughput Adaptation of the NADH-Coupled ATPase Assay for Screening Small Molecule Inhibitors

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Concanavalin A-Based Sedimentation Assay to Measure Substrate Binding of Glucan Phosphatases
09:07

Concanavalin A-Based Sedimentation Assay to Measure Substrate Binding of Glucan Phosphatases

Published on: December 23, 2022

结论:

  • 溶解和溶解效应在联体结合中起着重要作用,影响观察到的热力学概况.
  • 这些抑制剂的结合不仅仅是由最初假定的抑制剂化学决定的.
  • 这项工作提供了对控制抑制剂与甘酸酶结合的复杂因素的见解.