Formyline, a new glycation compound from the reaction of lysine and 3-deoxypentosone

Hellwig, Michael; Henle, Thomas

doi:10.1007/s00217-010-1237-3

Cited by 33 publications

(54 citation statements)

References 34 publications

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“…The water used for the preparation of buffers and solutions was obtained using a Purelab plus purification system (USFilter, Ransbach-Baumbach, Germany). Formyline [8] and pyrraline [20] were prepared according to the literature stated.…”

Section: Methodsmentioning

confidence: 99%

“…Formyline, a recently identified MRP with a pyrrole core, has only been measured in model incubations until now [8,22]. It was therefore the aim of this project to determine formyline in a broad range of more complex food samples.…”

Section: Development Of the Hplc Assaymentioning

confidence: 99%

“…A linear gradient from 3 to 13 % B in 30 min was applied at a flow rate of 1 mL/min. External calibration was performed with the standards synthesized as described in the literature [8,20]. The limits of detection (LOD) and quantification (LOQ), respectively, represent the concentrations of the analytes that are necessary to show a peak with signal-to-noise ratios of 3 and 10, respectively.…”

Section: Protein Hydrolysismentioning

confidence: 99%

“…Aliquots of the food samples representing 3-5 mg of protein were subjected to enzymatic hydrolysis as described previously [8,25]. The incubations were performed in a drying chamber at 37°C.…”

Section: Protein Hydrolysismentioning

confidence: 99%

“…1), which represent non-proteinogenic amino acids. Lysine derivatives with a pyrrole moiety like 6-(2-formyl-5-hydroxymethylpyrrol-1-yl)-Lnorleucine (Pyrraline) and 6-(2-formylpyrrol-1-yl)-L-norleucine (formyline) are formed during the reaction of 3-deoxyosones and amino compounds in a Paal-Knorr reaction [7][8][9]. Formyline has only recently been characterized for the first time [8].…”

Section: Introductionmentioning

confidence: 99%

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Quantification of the Maillard reaction product 6-(2-formyl-1-pyrrolyl)-l-norleucine (formyline) in food

Hellwig

Henle

2012

Eur Food Res Technol

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The Maillard reaction product 6-(2-formyl-1-pyrrolyl)-L-norleucine (formyline) was recently identified as a new pyrrole amino acid resulting from the reaction of free and protein-bound lysine residues with the 1,2-dicarbonyl compound 3-deoxypentosone, pentose sugars, and degradation products of disaccharides. In the present work, simultaneous analysis of formyline and its structural analog, pyrraline, in enzymatically hydrolyzed food matrices was achieved on an RP-phenyl column by high-pressure liquid chromatography (HPLC) with UV detection. The presence of formyline was for the first time unequivocally verified in the hydrolyzates and standard samples by HPLC coupled to triple quad mass spectrometry due to identity of product ion spectra after targeted fragmentation of the molecular ion of formyline. A total of 68 food samples were analyzed. Low concentrations of formyline were detected in milk and whey products. In breakfast cereals, pasta, and bakery products, formyline was quantified in concentrations up to 34.8 mg/kg. In the outmost bread crust, 0.6 % of lysine residues can be modified to formyline. Moreover, it was shown by analysis of concentrated beer samples that both formyline and pyrraline are constituents of beer proteins. From our data, we conclude that at least 2-3 mg of formyline and 20-40 mg of pyrraline are ingested with the daily diet.

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Section: Methodsmentioning

confidence: 99%

Section: Development Of the Hplc Assaymentioning

confidence: 99%

Section: Protein Hydrolysismentioning

confidence: 99%

Section: Protein Hydrolysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Quantification of the Maillard reaction product 6-(2-formyl-1-pyrrolyl)-l-norleucine (formyline) in food

Hellwig

Henle

2012

Eur Food Res Technol

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Transport of Free and Peptide‐Bound Glycated Amino Acids: Synthesis, Transepithelial Flux at Caco‐2 Cell Monolayers, and Interaction with Apical Membrane Transport Proteins

et al. 2011

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In glycation reactions, the side chains of protein-bound nucleophilic amino acids such as lysine and arginine are post-translationally modified to a variety of derivatives also known as Maillard reaction products (MRPs). Considerable amounts of MRPs are taken up in food. Here we have studied the interactions of free and dipeptide-bound MRPs with intestinal transport systems. Free and dipeptide-bound derivatives of N(6)-(1-fructosyl)lysine (FL), N(6)-(carboxymethyl)lysine (CML), N(6)-(1-carboxyethyl)lysine (CEL), formyline, argpyrimidine, and methylglyoxal-derived hydroimidazolone 1 (MG-H1) were synthesized. The inhibition of L-[(3)H]lysine and [(14) C]glycylsarcosine uptakes was measured in Caco-2 cells which express the H(+)/peptide transporter PEPT1 and lysine transport system(s). Glycated amino acids always displayed lower affinities than their unmodified analogues towards the L-[(3)H]lysine transporter(s). In contrast, all glycated dipeptides except Ala-FL were medium- to high-affinity inhibitors of [(14)C]Gly-Sar uptake. The transepithelial flux of the derivatives across Caco-2 cell monolayers was determined. Free amino acids and intact peptides derived from CML and CEL were translocated to very small extents. Application of peptide-bound MRPs, however, led to elevation (up to 80-fold) of the net flux and intracellular accumulation of glycated amino acids, which were hydrolyzed from the dipeptides inside the cells. We conclude 1) that free MRPs are not substrates for the intestinal lysine transporter(s), and 2) that dietary MRPs are absorbed into intestinal cells in the form of dipeptides, most likely by the peptide transporter PEPT1. After hydrolysis, hydrophobic glycated amino acids such as pyrraline, formyline, maltosine, and argpyrimidine undergo basolateral efflux, most likely by simple diffusion down their concentration gradients.

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Transformation of Free and Dipeptide‐Bound Glycated Amino Acids by Two Strains of Saccharomyces cerevisiae

et al. 2016

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The yeast Saccharomyces cerevisiae transforms branched-chain and aromatic amino acids into higher alcohols in the Ehrlich pathway. During microbiological culturing and industrial fermentations, this yeast is confronted with amino acids modified by reducing sugars in the Maillard reaction (glycation). In order to gain some preliminary insight into the physiological "handling" of glycated amino acids by yeasts, individual Maillard reaction products (MRPs: fructosyllysine, carboxymethyllysine, pyrraline, formyline, maltosine, methylglyoxal-derived hydroimidazolone) were administered to two strains of S. cerevisiae in a rich medium. Only formyline was converted into the corresponding α-hydroxy acid, to a small extent (10 %). Dipeptide-bound pyrraline and maltosine were removed from the medium with concomitant emergence of several metabolites. Pyrraline was mainly converted into the corresponding Ehrlich alcohol (20-60 %) and maltosine into the corresponding α-hydroxy acid (40-60 %). Five specific metabolites of glycated amino acids were synthesized and characterized. We show for the first time that S. cerevisiae can use glycated amino acids as a nitrogen source and transform them into new metabolites, provided that the substances can be transported across the cell membrane.

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Formyline, a new glycation compound from the reaction of lysine and 3-deoxypentosone

Cited by 33 publications

References 34 publications

Quantification of the Maillard reaction product 6-(2-formyl-1-pyrrolyl)-l-norleucine (formyline) in food

Quantification of the Maillard reaction product 6-(2-formyl-1-pyrrolyl)-l-norleucine (formyline) in food

Transport of Free and Peptide‐Bound Glycated Amino Acids: Synthesis, Transepithelial Flux at Caco‐2 Cell Monolayers, and Interaction with Apical Membrane Transport Proteins

Transformation of Free and Dipeptide‐Bound Glycated Amino Acids by Two Strains of Saccharomyces cerevisiae

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