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PubMed2002

Design, synthesis, and NMR structure of linear and cyclic oligomers containing novel furanoid sugar amino acids.

Sugar Amino Acids (SAAs) are sugar moieties containing at least one amino and one carboxyl group. The straightforward synthesis of two furanoid SAAs, 3-amino-3-deoxy-1,2-isopropylidene-alpha-D-ribofuranoic acid (f-SAA1) and 3-amino-3-deoxy-1,2-isopropylidene-alpha-D-allofuranoic acid (f-SAA2) starting from diacetone glucose, is described. These SAAs were used as structural templates aiming at new structures for peptidomimetic drug design. f-SAA1 resembles a beta-amino acid, whereas f-SAA2 is a gamma-amino acid mimetic. Thus, for the synthesis of the mixed, linear and cyclic oligomers of f-SAA1, beta-homo-glycine (beta-hGly, also called beta-alanine) was chosen as an amino acid counterpart, while for the oligomer of f-SAA2 gamma-amino butyric acid (GABA) was chosen. Fmoc-[f-SAA1-beta-hGly](3)-OH (3) and cyclo[f-SAA1-beta-hGly](3) (5) resemble linear and cyclic beta-peptides with a very different substitution pattern, compared with the beta-peptides known so far in the literature, whereas Fmoc-[f-SAA2-GABA](3)-OH (4) resembles a gamma-peptide. The linear f-SAA oligomers 3 and 4 were synthesized on the solid-phase using Fmoc strategy. 23 unambiguous interresidue NOE contacts (from a total of 76 NOE values), obtained from extensive NMR studies in C(3)CN, were used in subsequent simulated annealing and MD calculations, to elucidate the 12/10/12-helical structure of oligomer 3 in CH(3)CN. The results indicate that f-SAA1 strongly induces a secondary structure. A characteristic CD curve for the linear oligomer 3 is observed up to 75 degrees C in both CH(3)CN and CH(3)CN/H(2)O, even though 3 contains beta-hGly, which is known to destabilize helices. By contrast, 4 does not seem to form a stable conformation in solution. The cyclic SAA containing oligomer cyclo [f-SAA1-beta-hGly](3) (5) exhibits a C(3) symmetric conformation on the NMR chemical shift time scale.

Amino Acids↗
PubMed2000

Synthesis and conformational studies of peptidomimetics containing furanoid sugar amino acids and a sugar diacid.

Furanoid sugar amino acids (1) were synthesized and used as dipeptide isosteres to induce interesting turn structures in small linear peptides. They belong to a new variety of designed hybrid structures that carry both amino and carboxyl groups on rigid furanose sugar rings. Four such molecules, 6-amino-2,5-anhydro-6-deoxy-D-gluconic acid (3, Gaa) and its mannonic (4, Maa), idonic (5, Iaa), and a 3,4-dideoxyidonic (6, ddIaa) congeners were synthesized. The synthesis followed a novel reaction path in which an intramolecular 5-exo S(N)2 opening of the hexose-derived terminal aziridine ring in 2 by the gamma-benzyloxy oxygen with concomitant debenzylation occurred during pyridinium dichromate oxidation of the primary delta-hydroxyl group to carboxyl function, leading to the formation of furanoid sugar amino acid frameworks in a single step. Incorporation of these furanoid sugar amino acids into Leu-enkephalin replacing its Gly-Gly portion gave analogues 8-11. Detailed structural analysis of these molecules by circular dichroism (CD) and various NMR techniques in combination with constrained molecular dynamics (MD) simulations revealed that two of these analogues, 8a and 10a, have folded conformations composed of an unusual nine-membered pseudo beta-turn-like structure with a strong intramolecular H-bond between LeuNH --> sugarC3-OH. This, in turn, brings the two aromatic rings of Tyr and Phe in close proximity, a prerequisite for biological activities of opioid peptides. The analgesic activities of 8a,b determined by mouse hot-plate and tail-clip methods were similar to that of Leu-enkephalin methyl ester. The syn disposition of the beta-hydroxycarboxyl motif on the sugar rings appears to be the driving force to nucleate the observed turn structures in some of these molecules (8 and 10). Repetition of the motif on both sides of a furanose ring resulted in a novel molecular design of sugar diacid, 2,5-anhydro-D-idaric acid (7, Idac). Bidirectional elongation of the diacid moieties of 7 with identical peptide strands led to the formation of a C2-symmetric reverse-turn mimetic 12 which displayed a very ordered structure consisting of identical intramolecular H-bonds at two ends between LeuNH --> sugar-OH, the same as in 8 and 10.

Amino Acids↗
PubMed1968

Control of amino sugar metabolism in Escherichia coli and isolation of mutants unable to degrade amino sugars.

1. Growth of Escherichia coli on glucosamine results in an induction of glucosamine 6-phosphate deaminase [2-amino-2-deoxy-d-glucose 6-phosphate ketol-isomerase (deaminating), EC 5.3.1.10] and a repression of glucosamine 6-phosphate synthetase (l-glutamine-d-fructose 6-phosphate aminotransferase, EC 2.6.1.16); glucose abolishes these control effects. 2. Growth of E. coli on N-acetylglucosamine results in an induction of N-acetylglucosamine 6-phosphate deacetylase and glucosamine 6-phosphate deaminase, and in a repression of glucosamine 6-phosphate synthetase; glucose diminishes these control effects. 3. The synthesis of amino sugar kinases (EC 2.7.1.8 and 2.7.1.9) is unaffected by growth on amino sugars. 4. Glucosamine 6-phosphate synthetase is inhibited by glucosamine 6-phosphate. 5. Mutants of E. coli that are unable to grow on N-acetylglucosamine have been isolated, and lack either N-acetylglucosamine 6-phosphate deacetylase (deacetylaseless) or glucosamine 6-phosphate deaminase (deaminaseless). Deacetylaseless mutants can grow on glucosamine but deaminaseless mutants cannot. 6. After growth on glucose, deacetylaseless mutants have a repressed glucosamine 6-phosphate synthetase and a super-induced glucosamine 6-phosphate deaminase; this may be related to an intracellular accumulation of acetylamino sugar that also occurs under these conditions. In one mutant the acetylamino sugar was shown to be partly as N-acetylglucosamine 6-phosphate. Deaminaseless mutants have no abnormal control effects after growth on glucose. 7. Addition of N-acetylglucosamine or glucosamine to cultures of a deaminaseless mutant caused inhibition of growth. Addition of N-acetylglucosamine to cultures of a deacetylaseless mutant caused lysis, and secondary mutants were isolated that did not lyse; most of these secondary mutants had lost glucosamine 6-phosphate deaminase and an uptake mechanism for N-acetylglucosamine. 8. Similar amounts of (14)C were incorporated from [1-(14)C]-glucosamine by cells of mutants and wild-type growing on broth. Cells of wild-type and a deaminaseless mutant incorporated (14)C from N-acetyl[1-(14)C]glucosamine more efficiently than from N[1-(14)C]-acetylglucosamine, incorporation from the latter being further decreased by acetate; cells of a deacetylaseless mutant showed a poor incorporation of both types of labelled N-acetylglucosamine.

Bacteriolysis↗
PubMed2005

A gas chromatographic/mass spectrometric method for tracing the microbial conversion of glucose into amino sugars in soil.

Amino sugars in soils are heterogeneous and have been used as microbial residue biomarkers to investigate the microbial contribution to soil organic matter. However, it is not clear what the available carbon source is and how glucose is utilized for the synthesis of soil amino sugars. This paper presents a new gas chromatography/mass spectrometry (GC/MS) approach for the identification of 13C incorporation into three amino sugars, D-glucosamine, D-galactosamine, and muramic acid, in soil incubated with U-13C-glucose. Method evaluation showed that the chemical ionization (CI) mode was suitable for all these amino sugars, but that electron impact (EI) mode was applicable only to glucosamine and galactosamine. The 13C conversion rate was estimated based on the abundance ratio of the ions corresponding to the masses of the ions F+n and F (where n is the skeleton carbon number in the fragment ions F of the amino sugars) and calculated as atom percentage excess. The reproducibility of the method was excellent and clearly adequate for the present purpose. In addition, the new approach is highly accurate as tested with mixtures of U-13C-glucose and natural glucose.

Amino Sugars↗
PubMed2002

Evaluation of amino sugar, low molecular peptide and amino acid impurities of biotechnologically produced amino acids by means of CE.

As the second part of our studies on the impurity profiles of amino acids produced by biotechnological processes, a micellar electrokinetic chromatography (MEKC) was applied to determine amino sugars, low molecular peptides and amino acids as potential expected impurities at a level 0.1% w/w. 3-(4-Carboxybenzoyl)quinoline-2-carboxaldehyde (CBQCA) was found to be suitable as a labeling reagent for laser induced fluorescence (LIF) detection. The labeling reaction was optimized to achieve maximum reaction yields and reproducibility for all groups of substances. The 'level 0.1%' was chosen as quantities/concentrations in such a way that the major reagent peak becomes comparable with the impurities at this level, and the minor reagent peaks (<0.01%) are not able to cover other peaks at the level of interest. The reaction optimization and the validation studies were performed with model mixtures of representative amino sugars, low molecular peptides and amino acids. A linearity range of labeling of three orders of magnitude was achieved. The total precision of the method, including the labeling reproducibility was studied and for all test substances relative standard deviation less than 5% were obtained. The accuracy was evaluated by performing recovery experiments at three concentrations covered a 50-200% interval of the level 0.1%. Confidence intervals below +/-2.5% (lambda=0.05, n=9) of the target were found sufficient for purity tests.

Amino Acids↗
PubMed1983

A procedure for the separation and quantitation of tryptophan and amino sugars on the amino acid analyzer.

Tryptophan, 5-methyl tryptophan, glucosamine, and galactosamine can be separated from each other and hydrolysis products including lysinoalanine by chromatography on a 6 X 260-mm column of W-3H resin. The column is developed at 70 degrees C for 20 min with pH 3.95 (0.4 M Na+) buffer, followed by pH 6.4 (1 M Na+) buffer for 55 min using a Beckman 119 CL amino acid analyzer. The recovery of the internal standards, 5-methyl tryptophan and galactosamine, can then be used to correct for tryptophan and glucosamine losses, respectively. The procedure uses the column and buffers normally employed for protein hydrolysate analysis and does not require additional resin columns, special buffers, or flow rate changes.

Amino Sugars↗
PubMed1968

A new method for the quantitative determination of monosaccharides, amino sugars and N-acetylneuraminic acid and of 6-deoxyhexose (fucose) in the presence of other sugars.

1. Monosaccharides, amino sugars and N-acetylneuraminic acid were determined by using an original colorimetric assay procedure, based on the detection of formaldehyde released after periodate oxidation. A range of these compounds was investigated by this method and they were all found to obey Beer's law within the concentration range 0-0.6mumole/ml. 2. A simple method for the determination of 6-deoxyhexose concentration in the presence of other monosaccharides is also described. 3. The optimum pH for the release of formaldehyde from sugars by periodate oxidation was 7.0-7.5. 4. The methods described have considerable advantages over existing assay systems and their particlar value in automatic colorimetry, where the use of concentrated acids is undesirable, is discussed.

Amino Sugars↗
PubMed2006

Amino sugars: new inhibitors of zeaxanthin epoxidase, a violaxanthin cycle enzyme.

The effect of three sugars and their amino derivatives on violaxanthin cycle enzymes activity was investigated in duckweed (Lemna trisulca), a model water-plant. No effect of sugars and amino sugars on violaxanthin de-epoxidase was observed independent of incubation time; however, epoxidation of zeaxanthin to violaxanthin was inhibited. The minimum amino sugar concentrations causing maximum inhibition of zeaxanthin epoxidation have been estimated. Amino sugars but not sugars caused more than a 50% inhibition of zeaxanthin epoxidation in duckweed after a 24h incubation when applied at a concentration of 0.5%. Incubation with amino sugars under a 6d photoperiod enhanced the inhibitory effect. Zeaxanthin epoxidation was completely inhibited under such conditions, whereas only a minor inhibitory effect was observed in sugar treated plants. The strong amino sugar inhibition of zeaxanthin epoxidase activity represents additional evidence for the creation of an unstable carotenoid carbocation in the molecular mechanism of epoxidation.

Amino Sugars↗
PubMed1989

Suppression of human natural killer cell activity by amino sugars.

In the present study we investigated the effect of amino sugars on human natural killer (NK) activity against K562, a human myeloid leukemia cell line, and Molt-4, a human T lymphoma cell line. The presence of amino sugars such as D-mannosamine, D-galactosamine, and D-glucosamine [6-25 mM (in the case of D-mannosamine, 1.5-12.5 mM)] in a 4-hr chromium-51 (Cr) release assay significantly inhibited NK activity of large granular lymphocytes (LGL) without affecting effector cell viability or spontaneous release from target cells. Sugars with acetylated amino residues (N-acetyl-D-mannosamine, N-acetyl-D-galactosamine, and N-acetyl-D-glucosamine) showed much smaller NK inhibition. Among the amino sugars tested, D-mannosamine was the strongest suppressor. When either LGL or K562 cells were pretreated with amino sugars and used in the 4-hr 51Cr release assay, only the pretreatment of effector cells resulted in the reduction of NK activity. The binding capacity of LGL to K562 cells, determined by a conjugate assay, was not reduced by the amino sugars enough to explain the strong inhibition of NK activity by these amino sugars, although some inhibitory effect on the binding of LGL to K562 cells was observed in some cases. In contrast, the polarization of the effector cell cytoskeleton, one of the energy-dependent steps, was significantly impaired. The cellular ATP level of LGL was also significantly reduced and the reduction of cellular ATP correlated well with the degree of the inhibition of NK cytotoxicity. These results suggest that the suppression of NK activity by amino sugars is due to the reduction of the ATP-based energy supply of the effector cells and that amino sugars, especially D-mannosamine, should be recognized as potent suppressors of natural cell-mediated immunity.

Adenosine Triphosphate↗
PubMed1989

Change in specificity of glycosidase inhibition by N-alkylation of amino sugars.

The synthetic amino sugar 1,4-dideoxy-1,4-imino-L-allitol (DIA) is a moderately good inhibitor of human liver alpha-D-mannosidases and a weak inhibitor of alpha-L-fucosidase, N-acetyl-beta-D-hexosaminidase and beta-D-mannosidase. Methylation of the ring nitrogen of DIA markedly decreases the inhibition of all the glycosidases except N-acetyl-beta-D-hexosaminidase. N-Benzylation of DIA essentially abolishes all inhibitory activity, except towards alpha-L-fucosidase, which is more strongly inhibited than by either DIA or N-methyl-DIA. This is the first report of a change of specificity of inhibition of a glycosidase inhibitor by substitution of the ring nitrogen.

Benzyl Compounds↗
PubMed1984

Effect of amino sugars on platelet aggregation and on fibrinogen binding.

The amino sugars glucosamine, galactosamine and mannosamine (30 mM) inhibited aggregation of human or rabbit platelets induced by ADP, collagen, thrombin, PAF or high concentrations of sodium arachidonate. 125I-fibrinogen binding during ADP-induced aggregation, and release of amine storage granule contents were also inhibited. Increasing the calcium concentration of the suspending medium to 5 mM did not overcome the inhibitory effect on the release reaction. The amino sugars deaggregated rabbit platelets that had been aggregated by ADP, collagen or thrombin, but deaggregated human platelets readily only when ADP was used as the aggregating agent. Fibrinogen-induced aggregation of chymotrypsin-treated platelets was blocked by the amino sugars. They did not inhibit platelet adherence to a collagen-coated glass surface, nor affect release of granule contents from the adherent platelets. Aggregation and release induced by low concentrations of sodium arachidonate or the divalent cation ionophore A23187 were potentiated, indicating that the effects of the amino sugars on platelets are more complex than simple inhibition of the lectin-like activity that becomes available on the surface of platelets that have undergone the release reaction. One of the effects of the amino sugars, however, is interference with the binding of fibrinogen to platelets. The effects of the amino sugars are shared by other primary amines.

Adenosine Diphosphate↗