88125-05-7Relevant articles and documents
Development of a stable isotope dilution assay for an accurate quantification of protein-bound N(ε)-(1-deoxy-D-fructos-1-yl)-L-lysine using a 13C-labeled internal standard
Vinale,Fogliano,Schieberle,Hofmann
, p. 5084 - 5092 (1999)
Syntheses of the labeled Amadori compound [13C6]-N(ε)-(1-deoxy-D- fructos-1-yl)-L-lysine ([13C6]-DFLys) and the labeled glycated tetrapeptide Ala-[13C6]-DFLys-Leu-Gly are presented. The compounds were used in the development of stable isotope dilution assays for the quantification of the degree of glycosylation of bovine serum albumin treated for 20 min at 95 °C in the presence of glucose. The experiments revealed that the use of the labeled standards in combination with LC/MS allowed the exact quantification of protein-bound DFLys with the high recovery rate of 95% (at a spike level of 150 nmol/mg of protein) and a low detection limit of 5 nmol/mg of protein. The data revealed, however, that DFLys is significantly degraded during the enzymic hydrolysis of the protein backbone generally needed in the quantification procedure and, furthermore, incomplete digestion of the protein was observed. Both sources of errors were clearly overcome by using in particular the labeled peptide as the internal standard.
Lysine-Derived Protein-Bound Heyns Compounds in Bakery Products
Treibmann, Stephanie,Hellwig, Anne,Hellwig, Michael,Henle, Thomas
, p. 10562 - 10570 (2017)
Fructose and dicarbonyl compounds resulting from fructose in heated foods have been linked to pathophysiological pathways of several metabolic disorders. Up to now, very little has been known about the Maillard reaction of fructose in food. Heyns rearrang
Revisiting Amadori and Heyns synthesis: Critical percentage of acyclic form play the trick in addition to catalyst
Chanda, Debasree,Harohally, Nanishankar V.
supporting information, p. 2983 - 2988 (2018/06/29)
Amadori and Heyns reaction are landmark reactions of carbohydrate chemistry. Synthesis of simple Amadori and Heyns compounds are complicated by various factors and require tedious column chromatographic or ion chromatographic separations. Herein, we report an improved catalytic method based on classical synthetic method of Amadori and Heyns compounds in light of new understanding of a factor governing the reaction. By utilizing the improved catalytic method, we have accomplished several Amadori compounds of D-tagatose and also numerous other Amadori and Heyns compounds.
Transport of Free and Peptide-Bound Glycated Amino Acids: Synthesis, Transepithelial Flux at Caco-2 Cell Monolayers, and Interaction with Apical Membrane Transport Proteins
Hellwig, Michael,Geissler, Stefanie,Matthes, Rene,Peto, Anett,Silow, Christoph,Brandsch, Matthias,Henle, Thomas
, p. 1270 - 1279 (2012/04/04)
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 N6-(1-fructosyl)lysine (FL), N6-(carboxymethyl)lysine (CML), N6-(1-carboxyethyl)lysine (CEL), formyline, argpyrimidine, and methylglyoxal-derived hydroimidazolone 1 (MG-H1) were synthesized. The inhibition of L-[3H]lysine and [14C]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-[3H]lysine transporter(s). In contrast, all glycated dipeptides except Ala-FL were medium- to high-affinity inhibitors of [14C]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.
Formation of Aromatic Compounds from Carbohydrates. IX. Reaction of D-Glucose and L-Lysine in Slightly Acidic, Aqueous Solution
Miller, Raya,Olsson, Kjell,Pernemalm, Per-Ake
, p. 689 - 694 (2007/10/02)
The title reaction yielded 1-deoxy-1-(N6-lysino)-D-fructose, (+/-)-2-formyl-5-(hydroxymethyl)pyrrole-1-norleucine, the new 5-(3,4,5,6-tetrahydropyrid-3-ylidenemethyl)-2-furanmethanol and several compounds previously identified as products in the reaction of D-glucose with methylamine or glycine under similar conditions.The lysine slowly racemized during the reaction.Such racemization of amino acids might contribute to the nutritional loss caused by Maillard reactions in food.
