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相关概念视频

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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相关实验视频

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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
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一个驼类抗体片段抑制了由人类化酶形成粉样纤维的形成.

Mireille Dumoulin1, Alexander M Last, Aline Desmyter

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

Nature
|August 15, 2003
PubMed
概括

针对人体酶的驼虫抗体片段可以抑制粉样蛋白聚合. 这种方法恢复了蛋白质的结构完整性,为治疗蛋白质沉积疾病提供了一种策略.

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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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Immunization of Alpacas (Lama pacos) with Protein Antigens and Production of Antigen-specific Single Domain Antibodies
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Immunization of Alpacas (Lama pacos) with Protein Antigens and Production of Antigen-specific Single Domain Antibodies

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科学领域:

  • 生物化学 生物化学
  • 结构生物学 结构生物学
  • 免疫学 免疫学 免疫学

背景情况:

  • 粉样蛋白疾病涉及蛋白质错误折叠和聚合成纤维和斑块.
  • 非神经病的全身性粉症与人类酶基因的突变有关.

研究的目的:

  • 为了研究驼类抗体碎片在抑制氨基化蛋白质聚合的潜力.
  • 阐明抗体结合阻止D67H人类酶变体聚合的机制.

主要方法:

  • 一个单域驼类抗体碎片对抗野生类型的人类溶酶的生成.
  • 试验室聚合试验测试了抗体片段对D67H变体的抑制作用.
  • 结构研究以确定抗体-蛋白相互作用部位和机制.

主要成果:

  • 驼类抗体片段成功抑制了氨基化物D67H人类酶变体的体外聚合.
  • 结构分析显示,抗体与突变部位不同的表位结合.
  • 抗体结合恢复了溶酶蛋白中的结构合作性和长距离的构造效应.

结论:

  • 抑制部分展开的蛋白质物种的形成是对抗粉样蛋白聚合的有效策略.
  • 驼虫抗体碎片可以合理设计,以准和预防蛋白质沉积疾病.
  • 这项研究为amyloidosis和相关蛋白质病变提供了一种新的治疗方法.