验证ToF-SIMS用于分析糖氨酸氨基甘油的使用
Lorna K Milne1, Arya Ajay D/O Ajayakumar1, Imogen L Holyland1
1Advanced Materials and Healthcare Technology, University of Nottingham, NG7 2RD, UK; Nottingham GlycoAnalytics Hub, Biodiscovery Institute, Faculty of Medicine and Health Sciences and Faculty of Science, University of Nottingham, NG7 2RD, UK.
Carbohydrate polymers
|November 6, 2025
概括
飞行时间二次离子质谱法 (ToF-SIMS) 可以有效地区分糖氨基甘氨酸 (GAG) 和来自不同动物来源的肝素. 这种快速方法为检测肝素产品中的污染物提供了高灵敏度.
科学领域:
- 分析化学 分析化学
- 生物化学 生物化学
- 材料科学 材料科学 材料科学
背景情况:
- 葡萄糖氨基甘 (GAG) 具有多种生物功能,在制药中作为药物标或生物标志物至关重要.
- 肝素是一种重要的抗凝剂,主要来自猪,但多样化来源 (牛,羊) 对于减轻供应链风险至关重要.
- 准确地从各种动物来源的肝素中进行化学分化是一个重要的分析障碍.
研究的目的:
- 评估飞行时间二次离子质谱 (ToF-SIMS) 以进行来自不同动物来源的GAG和肝素的化学歧视.
- 建立ToF-SIMS作为一种敏感的方法,用于检测肝素制剂中的污染物.
主要方法:
- 在GAG样本上进行了ToF-SIMS分析,采用快速数据采集 (约. 每个样本1分钟) 和最低样本要求 (75 pg).
- 多变量分析 (MVA) 模型被用来解释ToF-SIMS数据进行分类和量化.
- 方法验证包括对特异性,精度,稳定性和量化极限的评估.
主要成果:
- 与MVA相结合的ToF-SIMS在区分GAG类型和肝素来源 (猪,牛,羊) 中实现了高选择性.
- 该方法在检测猪肝素中的GAG污染物中显示出高灵敏度,低至0.001重量% (羊肝素的0.01重量%).
- 该方法在特异性,精度,稳定性和量化方面得到了验证.
结论:
- ToF-SIMS是一种快速且高度敏感的分析技术,用于根据其类型和动物来源对GAG和肝素进行化学歧视.
- 该方法为质量控制提供了一个强大的平台,确保来自不同来源的肝素产品的纯度和安全性.
- 这些发现支持采用ToF-SIMS用于制药行业的常规分析,以管理肝素供应链多元化.
相关概念视频
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...
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...
6.8K
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
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


