TY - JOUR

T1 - Analysis of Chemically Labile Glycation Adducts in Seed Proteins: Case Study of Methylglyoxal-Derived Hydroimidazolone 1 (MG-H1)

AU - Antonova, Kristina

AU - Vikhnina, Maria

AU - Soboleva, Alena

AU - Mehmood, Tahir

AU - Heymich, Marie-Louise

AU - Leonova, Tatiana

AU - Bankin, Mikhail

AU - Lukasheva, Elena

AU - Gensberger-Reigl, Sabrina

AU - Medvedev, Sergei

AU - Smolikova, Galina

AU - Pischetsrieder, Monika

AU - Frolov, Andrej

N1 - Publisher Copyright: © 2019 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2019/8/1

Y1 - 2019/8/1

N2 - 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 N ε-(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.

AB - 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 N ε-(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.

KW - Advanced glycation end products (AGEs); enzymatic hydrolysis; glycation; methylglyoxalderived hydroimidazolone 1 (MG-H1); seeds; seed ageing; seed quality; sodium dodecyl sulfate (SDS)

KW - Advanced glycation end products (AGEs)

KW - Enzymatic hydrolysis

KW - Glycation

KW - Methylglyoxal-derived hydroimidazolone 1 (MG-H1)

KW - Seed ageing

KW - Seed quality

KW - Seeds

KW - Sodium dodecyl sulfate (SDS)

KW - seed ageing

KW - methylglyoxal-derived hydroimidazolone 1 (MG-H1)

KW - PROTEOME

KW - ARGININE RESIDUES

KW - ENDPRODUCTS AGES

KW - MASS-SPECTROMETRY

KW - IN-VITRO

KW - SKIN

KW - END-PRODUCTS

KW - seed quality

KW - sodium dodecyl sulfate (SDS)

KW - MAILLARD REACTION

KW - seeds

KW - SERUM

KW - enzymatic hydrolysis

KW - glycation

KW - CHROMATOGRAPHIC ASSAY

UR - http://www.scopus.com/inward/record.url?scp=85070744496&partnerID=8YFLogxK

UR - http://www.mendeley.com/research/analysis-chemically-labile-glycation-adducts-seed-proteins-case-study-methylglyoxalderived-hydroimid

U2 - 10.3390/ijms20153659

DO - 10.3390/ijms20153659

M3 - Article

C2 - 31357424

VL - 20

SP - 1

EP - 19

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 15

M1 - 3659

ER -