Application of phenylboronic acid modified hydrogel affinity chips for high-throughput mass spectrometric analysis of glycated proteins
| Autor: | Simone K. Frey, Florian J. Schweigert, Maksim V. Kvach, Sergey V. Gontarev, Vadim V. Shmanai |
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| Rok vydání: | 2006 |
| Předmět: |
Glycation End Products
Advanced Proteomics Protein Array Analysis Mass spectrometry Ligands Fluorescence Mass Spectrometry Analytical Chemistry chemistry.chemical_compound Cyanogen Bromide Phenylboronic acid Spectroscopy Glycoproteins Chromatography Sepharose Organic Chemistry Hydrogels Boronic Acids Matrix-assisted laser desorption/ionization chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Self-healing hydrogels Proteome Agarose Cyanogen bromide Indicators and Reagents Spectrophotometry Ultraviolet Aluminum |
| Zdroj: | Rapid communications in mass spectrometry : RCM. 21(1) |
| ISSN: | 0951-4198 |
| Popis: | The complexity of the human plasma proteome is greatly increased by post-translational modifications. Besides physiological modifications, pathological conditions such as diabetes are responsible for adding to this complexity by producing advanced glycation endproducts (AGEs). When searching for specific biomarkers it is a prerequisite to reduce this complexity prior to analysis. To do this, agarose hydrogel was used to create a high-capacity affinity layer on the modified aluminum surface of MALDI (matrix-assisted laser desorption/ionization) targets. 3-Aminophenylboronic acid was immobilized via cyanogen bromide activation as a ligand for affinity sorption of glycated proteins, followed by their direct detection by MALDI. High protein capacity of prepared MALDI chips, efficient separation and low non-specific protein binding were demonstrated. The results show that phenylboronic acid modified hydrogels are very suitable for creating affinity surfaces for the high-throughput analysis of AGEs. |
| Databáze: | OpenAIRE |
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