期刊
ANALYTICAL CHEMISTRY
卷 94, 期 22, 页码 7909-7917出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.2c00681
关键词
-
D-glucose and D-fructose in mammals can react with amino groups, leading to glycated proteins. Metabolic diseases like diabetes elevate sugar levels, favoring glycation and the formation of advanced glycation end products (AGEs) linked to complications. Current analytical methods for differentiating and quantifying Amadori- and Heyns-modified proteins in complex samples are limited.
D-glucose and D-fructose present in blood, tissues, and organs of all mammals can react with amino groups, leading to glucated (Amadori) and fructated (Heyns) products, i.e., proteins glycated at lysine residues. While typically present at low concentration in humans, metabolic diseases including diabetes elevate sugar levels, favoring glycation and consecutive reactions leading to advanced glycation end products (AGEs) linked to diabetic complications and cardiovascular diseases. Analytical methods able to differentiate and to individually quantify Amadori- and Heyns-modified proteins in complex sample mixtures, e.g., serum, are still very limited. Here, we show that the reported and supposedly specific neutral losses displayed in tandem mass spectra of Heyns peptides cannot be used for a reliable differentiation as they were also observed for Amadori peptides. However, the combination of several neutral loss signals in fragment ion ratios at both precursor and fragment ion signals allowed the differentiation and relative quantitation of coeluting isomeric Amadori and Heyns peptides at different concentrations and peptide ratios. This was also true for digested human plasma. Thus, the presented strategy allows the quantitation of Amadori and Heyns peptides in complex samples, especially by spiking isotope-labeled peptides. This will allow searching for glucated and fructated biomarkers in clinical samples.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据