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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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Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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Proteoglycans01:05

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Glycosaminoglycans01:23

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Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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可调节的多价值Fe (II) 基甘油组合作为本地高曼诺斯甘的模仿剂.

Emerson Hall1, Yu-Shien Sung2, Chad W Priest2

  • 1Department of Biochemistry and Molecular Biophysics, University of California San Diego, La Jolla CA.

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概括

化学定义的多价值甘氨酸显示模仿高曼诺糖甘氨酸 (HMGs) 并抑制莱克结合. 这些Fe (II) 胺胺复合体为生物应用提供可调节的相互作用.

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科学领域:

  • 碳水化合物化学 碳水化合物化学
  • 生物物理化学 生物物理化学
  • 葡萄糖生物学 葡萄糖生物学

背景情况:

  • 高曼诺糖甘 (HMGs) 在蛋白质折叠和免疫等生物过程中至关重要.
  • 莱克通过多价值相互作用结合HMG,涉及多种糖和莱克结合部位.

研究的目的:

  • 使用Fe(II) 胺基胺复合物创建化学定义的多价值甘氨酸显示器.
  • 为了研究这些显示器与单体格里菲辛 (mGRFT) 作为模型讲解素的相互作用.
  • 探索它们作为HMG模仿剂和竞争性抑制剂的潜力.

主要方法:

  • 合成Fe(II) 胺基胺复合物,控制糖甘价值,臂长和曼诺斯显示.
  • 使用生物层干扰测量 (BLI),异热定位热量测量 (ITC) 和NMR光谱学进行相互作用的表征.
  • 系统的分子修改来调整结合亲和力.

主要成果:

  • 铁基组件的结合亲和力 (KD) 与mGRFT的结合亲和力在1000倍以上的范围内.
  • 结合亲和力可以通过改变糖长度和显示糖的数量来调整.
  • 证明了这些组件模仿本土HMG的能力.

结论:

  • 可调节的Fe (II) 甘组件作为高曼诺斯甘的有效模仿剂.
  • 这些组合可以作为竞争性抑制剂,抑制本地糖甘因与莱克结合.
  • 该研究为设计具有受控结合性质的基甘基分子提供了一个平台.