Analysis of Chemically Labile Glycation Adducts in Seed Proteins: Case Study of Methylglyoxal-Derived Hydroimidazolone 1 (MG-H1).

Antonova K, Vikhnina M, Soboleva A, Mehmood T, Heymich ML, Leonova T, Bankin M, Lukasheva E, Gensberger-Reigl S, Medvedev S, Smolikova G, Pischetsrieder M, Frolov A (2019)

Publication Status: Published

Publication Type: Journal article

Publication year: 2019

Journal

International Journal of Molecular Sciences MDPI

Book Volume: 20

Article Number: 3659

Journal Issue: 15

URI: https://www.mdpi.com/1422-0067/20/15/3659

DOI: 10.3390/ijms20153659

Open Access Link: https://www.mdpi.com/1422-0067/20/15/3659

Abstract

Seeds represent the major source of food protein, impacting on both human nutrition and animal feeding. Therefore, seed quality needs to be appropriately addressed in the context of viability and food safety. Indeed, long-term and inappropriate storage of seeds might result in enhancement of protein glycation, which might affect their quality and longevity. Glycation of seed proteins can be probed by exhaustive acid hydrolysis and quantification of the glycation adduct Nepsilon-(carboxymethyl)lysine (CML) by liquid chromatography-mass spectrometry (LC-MS). This approach, however, does not allow analysis of thermally and chemically labile glycation adducts, like glyoxal-, methylglyoxal- and 3-deoxyglucosone-derived hydroimidazolones. Although enzymatic hydrolysis might be a good solution in this context, it requires aqueous conditions, which cannot ensure reconstitution of seed protein isolates. Because of this, the complete profiles of seed advanced glycation end products (AGEs) are not characterized so far. Therefore, here we propose the approach, giving access to quantitative solubilization of seed proteins in presence of sodium dodecyl sulfate (SDS) and their quantitative enzymatic hydrolysis prior to removal of SDS by reversed phase solid phase extraction (RP-SPE). Using methylglyoxal-derived hydroimidazolone 1 (MG-H1) as a case example, we demonstrate the applicability of this method for reliable and sensitive LC-MS-based quantification of chemically labile AGEs and its compatibility with bioassays.

Authors with CRIS profile

Marie-Louise Heymich Lehrstuhl für Lebensmittelchemie (Henriette-Schmidt-Burkhardt Lehrstuhl) Sabrina Gensberger-Reigl Lehrstuhl für Lebensmittelchemie (Henriette-Schmidt-Burkhardt Lehrstuhl) Monika Pischetsrieder Lehrstuhl für Lebensmittelchemie (Henriette-Schmidt-Burkhardt Lehrstuhl)

Involved external institutions

Saint Petersburg State University (SPbU) / Санкт-Петербургский государственный университет (СПбГУ) RU Russian Federation (RU) Leibniz Institute of Plant Biochemistry / Leibniz-Institut für Pflanzenbiochemie DE Germany (DE)

How to cite

APA:

Antonova, K., Vikhnina, M., Soboleva, A., Mehmood, T., Heymich, M.-L., Leonova, T.,... Frolov, A. (2019). Analysis of Chemically Labile Glycation Adducts in Seed Proteins: Case Study of Methylglyoxal-Derived Hydroimidazolone 1 (MG-H1). International Journal of Molecular Sciences, 20(15). https://doi.org/10.3390/ijms20153659

MLA:

Antonova, Kristina, et al. "Analysis of Chemically Labile Glycation Adducts in Seed Proteins: Case Study of Methylglyoxal-Derived Hydroimidazolone 1 (MG-H1)." International Journal of Molecular Sciences 20.15 (2019).

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