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相关概念视频

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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相关实验视频

Updated: Jan 14, 2026

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy
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Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy

Published on: February 7, 2025

984

增加L-SIGN特异性糖仿制剂的化学空间

Gianluca Cavazzoli1, Clara Delaunay2, Sara Pollastri1

  • 1Dipartimento di Chimica, Università degli Studi di Milano, via Golgi 19, Milano 20133, Italy.

Journal of medicinal chemistry
|October 18, 2025
PubMed
概括

研究人员开发了新的曼诺斯糖仿制剂,这些药物与L-SIGN结合,L-SIGN是一种C型莱克受体. 这些化合物对L-SIGN具有很高的选择性,与以前版本的潜在抗病毒疗法相匹配或改进.

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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
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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
  • 药物发现 药物发现 药物发现

背景情况:

  • 像L-SIGN这样的C型莱克受体是抗病毒疗法和药物输送的目标.
  • 之前的研究发现Man84是一种具有微分子亲和力的选择性L-SIGN配体.
  • 对同类讲解蛋白 (如DC-SIGN) 的高选择性至关重要.

研究的目的:

  • 设计和合成具有维持或改善L-SIGN选择性的新型Man84同位素 (连接体2-11).
  • 评估这些新配体对L-SIGN和DC-SIGN的结合亲和力和选择性.
  • 阐明对L-SIGN结合的连接体的结构基础.

主要方法:

  • 合成Man84同位素 (连接体2-11).
  • 表面等离子体共振 (SPR) 抑制试验使用固定SARS-CoV-2尖端蛋白来测量L-SIGN和DC-SIGN的结合亲和力和选择性.
  • 进行X射线晶体学以确定L-SIGN CRD/连接体4复合体的结构.

主要成果:

  • 化合物4,5和9对L-SIGN的微分子亲和力较低.
  • 这些化合物对L-SIGN比DC-SIGN具有50-94倍的选择性,匹配或超过Man84.
  • 晶体结构揭示了连接物4和L-SIGN残留物E370.0之间的关键双酸键相互作用.

结论:

  • 开发出来的Man84异质体代表有力的和有选择性的L-SIGN配体.
  • 这些发现支持这些化合物在抗病毒策略和有针对性的输送系统中的潜力.
  • 结构洞察力为进一步优化L-SIGN向配体提供了基础.