Dataset Information

Isolation, purification and characterization of histidino-threosidine, a novel Maillard reaction protein crosslink from threose, lysine and histidine.

ABSTRACT: We isolated a novel acid-labile yellow chromophore from the incubation of lysine, histidine and d-threose and identified its chemical structure by one and two-dimensional NMR spectroscopy combined with LC-tandem mass spectrometry. This new cross-link exhibits a UV absorbance maximum at 305 nm and a molecular mass of 451 Da. The proposed structure is 2-amino-5-(3-((4-(2-amino-2-carboxyethyl)-1H-imidazol-1-yl)methyl)-4-(1,2-dihydroxyethyl)-2-formyl-1H-pyrrol-1-yl)pentatonic acid, a cross-link between lysine and histidine with addition of two threose molecules. It was in part deduced and confirmed through synthesis of the analogous compound from n-butylamine, imidazole and d-threose. We assigned the compound the trivial name histidino-threosidine. Systemic incubation revealed that histidino-threosidine can be formed in low amounts from fructose, glyceraldehyde, methylglyoxal, glycolaldehyde, ascorbic acid, and dehydroascorbic acid, but at a much higher yield with degradation products of ascorbic acid, i.e. threose, erythrose, and erythrulose. Bovine lens protein incubated with 10 and 50 mM threose for two weeks yielded 560 and 2840 pmol/mg histidino-threosidine. Histidino-threosidine is to our knowledge the first Maillard reaction product known to involve histidine in a crosslink.

SUBMITTER: Dai Z

PROVIDER: S-EPMC1978223 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature

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Isolation, purification and characterization of histidino-threosidine, a novel Maillard reaction protein crosslink from threose, lysine and histidine.

Dai Zhenyu Z Nemet Ina I Shen Wei W Monnier Vincent M VM

Archives of biochemistry and biophysics 20070402 1

We isolated a novel acid-labile yellow chromophore from the incubation of lysine, histidine and d-threose and identified its chemical structure by one and two-dimensional NMR spectroscopy combined with LC-tandem mass spectrometry. This new cross-link exhibits a UV absorbance maximum at 305 nm and a molecular mass of 451 Da. The proposed structure is 2-amino-5-(3-((4-(2-amino-2-carboxyethyl)-1H-imidazol-1-yl)methyl)-4-(1,2-dihydroxyethyl)-2-formyl-1H-pyrrol-1-yl)pentatonic acid, a cross-link betw ...[more]

PMID: 17466255

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Project description:Glucose-lysine based Maillard reaction products (MRPs) are introduced to the human body via food ingestion or are synthesized in vivo. Depending on reaction conditions, they represent a mixture of compounds with diverse chemical structures and physiological properties. MRPs may also be a potential nutrient source for Salmonella, a major foodborne gastrointestinal pathogen. This study was designed to determine the growth and transcriptional responses of S. Typhimurium LT2 to MRPs generated at low water activity to simulate the reaction occurring during food processing and storage. Maillard reactions between N-α-acetyl-lysine and glucose were varied in time (4, 23, and 143 h) to generate sub-samples with prevailing Amadori compound, advanced glycation end products (AGEs), or melanoidines respectively. The addition of MRP up to 5 mg mL-1 to defined media with 0.4% glucose had no effect on S. Typhimurium LT2 growth. In media, where the MRP sub-samples (4 and 23 h) served as the only carbon source, MRP assimilation by S. Typhimurium LT2 was observed as secondary logarithmic growth phases (0.063 h-1 and 0.072 h-1) after the growth on glucose available in the MRP reaction mixtures (0.479 h-1). The MRPs sub-sample with the highest concentration of melanoidines (143 h) also supported S. Typhimurium LT2 growth (0.368 h-1). Of the three MRPs sub-samples, the Amadori compound was the preferred carbon source for S. Typhimurium LT2 as evidenced by its almost complete disappearance (98%). Decreases in AGEs (37%) and melanoidines (15%), when incubated with S. Typhimurium LT2, also occurred. Transcription profiles of the cells grown on the MRPs fractions revealed predominant up-regulation of genes associated with the functional groups of energy metabolism, fatty and phospholipid metabolism, cellular process, and regulatory functions, and general down-regulation of the genes in the groups of amino acid biosynthesis, protein synthesis and transcription, transport and binding proteins, and DNA metabolism. The carbon flow in tricarboxylic acid (TCA) cycle partitioned by the glyoxylate cycle appeared to play an essential role in the assimilation of glucose-lysine-derived MRPs. The high expression level of numerous genes encoding hypothetical proteins or proteins with unknown function suggested the presence of genes whose role in glucose-lysine MRPs catabolism in Salmonella remains to be determined.

Project description:Glucose-lysine based Maillard reaction products (MRPs) are introduced to the human body via food ingestion or are synthesized in vivo. Depending on reaction conditions, they represent a mixture of compounds with diverse chemical structures and physiological properties. MRPs may also be a potential nutrient source for Salmonella, a major foodborne gastrointestinal pathogen. This study was designed to determine the growth and transcriptional responses of S. Typhimurium LT2 to MRPs generated at low water activity to simulate the reaction occurring during food processing and storage. Maillard reactions between N-Î±-acetyl-lysine and glucose were varied in time (4, 23, and 143 h) to generate sub-samples with prevailing Amadori compound, advanced glycation end products (AGEs), or melanoidines respectively. The addition of MRP up to 5 mg mL-1 to defined media with 0.4% glucose had no effect on S. Typhimurium LT2 growth. In media, where the MRP sub-samples (4 and 23 h) served as the only carbon source, MRP assimilation by S. Typhimurium LT2 was observed as secondary logarithmic growth phases (0.063 h-1 and 0.072 h-1) after the growth on glucose available in the MRP reaction mixtures (0.479 h-1). The MRPs sub-sample with the highest concentration of melanoidines (143 h) also supported S. Typhimurium LT2 growth (0.368 h-1). Of the three MRPs sub-samples, the Amadori compound was the preferred carbon source for S. Typhimurium LT2 as evidenced by its almost complete disappearance (98%). Decreases in AGEs (37%) and melanoidines (15%), when incubated with S. Typhimurium LT2, also occurred. Transcription profiles of the cells grown on the MRPs fractions revealed predominant up-regulation of genes associated with the functional groups of energy metabolism, fatty and phospholipid metabolism, cellular process, and regulatory functions, and general down-regulation of the genes in the groups of amino acid biosynthesis, protein synthesis and transcription, transport and binding proteins, and DNA metabolism. The carbon flow in tricarboxylic acid (TCA) cycle partitioned by the glyoxylate cycle appeared to play an essential role in the assimilation of glucose-lysine-derived MRPs. The high expression level of numerous genes encoding hypothetical proteins or proteins with unknown function suggested the presence of genes whose role in glucose-lysine MRPs catabolism in Salmonella remains to be determined. This study was designed to determine the growth and transcriptional responses of S. Typhimurium LT2 to MRPs generated at low water activity to simulate the reaction occurring during food processing and storage. Maillard reactions between N-Î±-acetyl-lysine and glucose were varied in time (4, 23, and 143 h) to generate sub-samples with prevailing Amadori compound, advanced glycation end products (AGEs), or melanoidines respectively. Total bacterial RNA was isolated as previously described and the RNA samples were then converted to fluorescently-labeled cDNA and hybridized to S. Typhimurium microarrays version 5 (NIAID's Pathogen Functional Genomics Resource Center). Real-time PCR and physiological experiments were performed to validate the microarray data. In all supplementary files channel A = Cy3, channel B = Cy5.

Dataset Information

Isolation, purification and characterization of histidino-threosidine, a novel Maillard reaction protein crosslink from threose, lysine and histidine.

Publications

Isolation, purification and characterization of histidino-threosidine, a novel Maillard reaction protein crosslink from threose, lysine and histidine.

Similar Datasets

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