Planta Med 2019; 85(18): 1508-1509
DOI: 10.1055/s-0039-3399947
Main Congress Poster
Poster Session 2
© Georg Thieme Verlag KG Stuttgart · New York

AGEs (advanced glycation end products): an advanced method for an advanced problem

S Velichkova
1   NatuRA (Natural Products and Food – Research and Analysis), Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp,, Universiteitsplein 1, 2610 Antwerp, Belgium
,
M Theunis
1   NatuRA (Natural Products and Food – Research and Analysis), Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp,, Universiteitsplein 1, 2610 Antwerp, Belgium
,
K Foubert
1   NatuRA (Natural Products and Food – Research and Analysis), Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp,, Universiteitsplein 1, 2610 Antwerp, Belgium
,
L Pieters
1   NatuRA (Natural Products and Food – Research and Analysis), Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp,, Universiteitsplein 1, 2610 Antwerp, Belgium
› Author Affiliations
Further Information

Publication History

Publication Date:
20 December 2019 (online)

 

Advanced glycation end products (AGEs) are heterogeneous, sugar-derived protein modifications [Fig.1] that have received attention in various research fields, such as food preparation, the normal aging process and pathophysiological conditions in the human body. [1]

Several in vitro experiments are reported to identify AGEs inhibitors, for instance: measuring glycation of bovine serum albumin, determination of fructosamine adducts and measuring α-dicarbonyl compounds. [2] However, the latter methods suffer from various drawbacks like a complex formation between test products and the protein can result in quenching of the fluorescence signal and misinterpretation of the data. Therefore, it was of utmost importance to develop and validate a reliable and universal method to circumvent these problems. Subsequently, several classes of natural products will be tested in the new method for their AGEs inhibition properties.

In this research, the precise quantification of N(6)-carboxymethyllysine (CML), one of the most abundant AGEs [3], was achieved through HILIC Ultra-Performance Liquid Chromatography coupled to a Xevo G2-XS QTof MS system, using d2-CML as an internal standard. CML was generated by incubation of GK-peptide and ribose. The sample preparation included a hydrolysis step with hydrochloric acid and a clean up step with P3 (Protein Precipitation Plate) cartridges. The method was validated following the FDA guidelines of Bioanalytical Method Validation [4] regarding linearity, LLOQ, precision and quality controls.

Overall, advanced glycation is a leading cause for the progression and pathogenesis of many chronic diseases (e.g. diabetes mellitus). Specifically, this validated method can contribute to the unambiguous discovery of new potential anti-AGEs agents.

Zoom Image
Fig. 1 General scheme of AGEs formation.
 

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