化寡糖的化学修饰以功能化纳米结构脂质载体:探索两种不同的策略

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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

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Paul Rivollier1,2, Emeline Richard1, Antoine Hoang2

  • 1Univ. Grenoble Alpes, CNRS, CERMAV, 38000 Grenoble, France. sebastien.fort@cermav.cnrs.fr.

Organic & biomolecular chemistry
|May 8, 2025
PubMed
概括

研究人员开发了两种方法,以N-乙-神经氨基酸 (Neu5Ac) 功能化纳米结构脂质载体 (NLCs),用于向治疗. 接种方法产生了安全的NLC,有可能用于对抗流感病毒等病原体的抗粘合治疗.

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Protein Glycosylation01:25

Protein Glycosylation

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.
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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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