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関連する概念動画

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.5K
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...
9.2K
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

7.7K
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

Proteoglycans

4.6K
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,...
4.6K
Glycosaminoglycans01:23

Glycosaminoglycans

6.8K
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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関連する実験動画

Updated: Jan 7, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
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ネイティブの高マンノース糖鎖を模倣する調整可能な多価Fe(II)ベースのグリコアセンブリ

Emerson Hall1, Yu-Shien Sung2, Chad W Priest2

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

bioRxiv : the preprint server for biology
|December 25, 2025
PubMed
まとめ

化学的に定義された多価糖鎖ディスプレイは、高マンノース糖鎖（HMG）を模倣し、レクチン結合を阻害する。これらのFe(II)イミノピリジン錯体は、生物学的応用に向けて調整可能な相互作用を提供する。

キーワード:
Fe(II)錯体グリコアセンブリ高マンノース糖鎖レクチン糖鎖模倣多価相互作用結合親和性バイオレイヤー干渉法等温滴定熱量測定

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関連する実験動画

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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
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科学分野:

  • 炭水化物化学
  • 物理化学
  • 糖鎖生物学

背景:

  • 高マンノース糖鎖（HMG）は、タンパク質折り畳みや免疫などの生物学的プロセスにおいて重要です。
  • レクチンは、複数の糖とレクチン結合部位を含む多価相互作用を介してHMGに結合します。

主な方法:

  • 制御された糖鎖価、アーム長、マンノース表示を持つFe(II)イミノピリジン錯体の合成。
  • バイオレイヤー干渉法（BLI）、等温滴定熱量測定（ITC）、およびNMR分光法を用いた相互作用の特性評価。
  • 結合親和性を調整するための系統的な分子改変。

結論:

  • 調整可能なFe(II)糖鎖アセンブリは、高マンノース糖鎖の効果的な模倣物として機能します。
  • これらのアセンブリは、レクチンによるネイティブ糖鎖結合の競合阻害剤として機能することができます。
  • この研究は、制御された結合特性を持つ糖鎖ベースの分子の設計のためのプラットフォームを提供します。