糖化增强蛋白质与脂质双层膜的关联
Beatrice Barletti1,2, Nicoló Paracini3, Giovanna Fragneto3
1Université Grenoble-Alpes, CNRS, Grenoble INP, TIMC/SyNaBi (UMR 5525), Grenoble 38000, France.
Langmuir : the ACS journal of surfaces and colloids
|November 12, 2025
概括
糖化,一种与糖尿病相关的过程,增强了蛋白质与负电荷细胞膜的结合. 这一发现影响了对血液中的蛋白质行为的理解以及生物标志物的可靠性.
科学领域:
- 生物化学 生物化学
- 生物物理学的生物物理.
- 材料科学 材料科学 材料科学
背景情况:
- 糖化是一种非酶体修饰,形成先进的糖化最终产品 (AGEs),涉及糖尿病.
- 糖化蛋白可能与脂质接口的相互作用发生变化,影响生物分布和诊断准确性.
- 牛血清白蛋白 (BSA) 和其糖化形式 (gBSA) 作为蛋白质-脂质相互作用的模型.
研究的目的:
- 调查糖化如何影响BSA与脂质双层的相互作用.
- 了解膜电荷和流动性对蛋白质-糖化相互作用的影响.
- 为了阐明在糖化时蛋白质-脂质相互作用中的纳米结构变化.
主要方法:
- 利用不同组成的支持性脂质双层 (SLB) 来建模细胞膜.
- 采用中子反射计 (NR) 来比较BSA和gBSA的膜协会.
- 分析了双层界面上的纳米结构变化和蛋白质体积分数.
主要成果:
- BSA和gBSA与zwitterionic或cationic膜的相互作用是最小的.
- 观察到BSA和gBSA对负电荷双层的显著结合.
- 糖化显著放大了蛋白质-脂质相互作用,使膜相关蛋白质体积分数从0.11 (BSA) 增加到0.17 (gBSA).
结论:
- 糖化改变了蛋白质表面的特性,促进了与负电荷膜的更强的相互作用.
- 蛋白质-糖化-脂质相互作用是脂质依赖的,影响蛋白质的生物可用性和行为.
- 这些发现强调需要考虑糖化对蛋白质-脂质相互作用的影响,以确定生物标志物可靠性和糖尿病病理生理学.
相关概念视频
Protein Glycosylation
9.2K
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...
Glycosylation occurs in...
9.2K
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
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...
Multiple sugar molecules that may or may...
3.5K
Protein Modifications in the RER
6.8K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
6.8K
Amyloid Fibrils
11.5K
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,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
11.5K
Lipids as Anchors
7.1K
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
7.1K


