Thermal study of l-alanine, l-threonine, and taurine crystals related to hydrogen bonding

In this study l-alanine, l-threonine, and taurine crystals were characterized through dilatometric technique and thermogravimetric and differential thermal analysis. The dilatometric analysis shows that the thermal expansion of the crystals is correlated with the strengths of local hydrogen bonding in the amino acid structures at room temperature. Thermogravimetric analysis and differential thermal analysis of the l-alanine, taurine, and l-threonine crystals have been performed at high temperatures. No clear correlation between the hydrogen bonding strengths and endothermic peak positions was observed.     

Volumetric Properties of l-Alanine and l-Serine in Aqueous N,N-Dimethylformamide Solutions at 298.15 K

The densities of l-alanine and l-serine in aqueous solutions of N,N-dimethylformamide (DMF) have been measured at 298.15 K with an Anton Paar Model 55 densimeter. Apparent molar volumes $ (V_{\phi } ) $ ( V ? ) , standard partial molar volumes $ (V_{\phi }^{0} ) $ ( V ? 0 ) , standard partial molar volumes of transfer $ (\Updelta_{\text{tr}} V_{\phi }^{0} ) $ ( Δ tr V ? 0 ) and hydration numbers have been determined for the amino acids. The $ \Updelta_{\text{tr}} V_{\phi }^{0} $ Δ tr V ? 0 values of l-serine are positive which suggest that hydrophilic–hydrophilic interactions between l-serine and DMF are predominant. The –CH₃ group of l-alanine has much more influence on the volumetric properties and the $ \Updelta_{\text{tr}} V_{\phi }^{0} $ Δ tr V ? 0 have smaller negative values. The results have been interpreted in terms of the cosphere overlap model.     

Arenesulfonylation of dl-serine, l-proline, l-threonine, and dl-methionine in systems 1,4-dioxane—water and propan-2-ol—water

Kinetics of interaction of dl-serine, l-proline, l-threonine, and dl-methionine with 3-nitrobenzenesulfonyl chloride in water (40%)—1,4-dioxane and water (40%)—isopropanol mixed solvents was studied spectrophotometrically at 298 K. The main reactive form of α-amino acids is shown to be anionic. Under conditions of arenesulfonylation, the basicity of α-amino acids is crucial in determining the reaction rate. Arenesulfonylation rate constants are 20—50 times lower than the constants of N-acylation of the same α-amino acids with benzoyl chloride and 10⁴–10⁵ times higher than the rate constants of their reactions with benzoic acid 4-nitrophenyl ester.     

Biomimetic synthesis of calcium carbonate with different morphologies under the direction of different amino acids

Using three different amino acids (AAs) as organic matrices, including the highly nonpolar hydrophobic l-valine, the positively charged l-arginine and the less polar uncharged l-serine, calcium carbonate (CaCO₃) with different morphologies and polymorphs were synthesized by a facile gas diffusion reaction based on biomimetic strategy. Compared with the control cubic calcite obtained in the absence of AAs, the product from l-valine was cubic calcite aggregates assembled by nano-platelets. The product from l-arginine was spherical vaterite aggregates assembled by spherical nanoparticles. The product from l-serine was the mixture of cubic calcite and spherical vaterite. The structures and properties of the side chains of the AAs exerted the significant effects on the nucleation and growth of the CaCO₃. The formation mechanisms of the CaCO₃ in the presence of AAs are preliminarily discussed. The results suggest that the polymorphs and morphologies of the inorganic nanomaterials might be easily adjusted through the careful selection of the organic matrices.     

Comparison of ordered mesoporous materials sorption properties towards amino acids

The adsorption of amino acids such as l-phenylalanine and l-histidine was carried out on a series of mesoporous carbons obtained with the use ordered silicas KIT-6, SBA-16, SBA-15 as templates and furfuryl alcohol as carbon precursor. Small angle XRD analysis confirmed the ordered mesoporous structures of all materials obtained. They were also characterised by well-developed surface areas and high pore volumes. Adsorption behaviour of amino acids on ordered mesoporous carbons was investigated in potassium phosphate buffer solutions with adjustable l-phenylalanine and l-histidine concentration, ion strength, and pH. The highest sorption capacity towards the amino acids were observed at pH close to the isoelectric point of l-phenylalanine (pI = 5.48) and l-histidine (pI = 7.59). Electrostatic, hydrophobic and steric interactions had very strong effect on the adsorption of amino acids on mesoporous carbons. The amount of l-phenylalanine and l-histidine adsorbed decreased in the following sequence: C_KIT-6 > C_SBA-16 > C_SBA-15 that was strongly related to their structure, surface areas and average pore diameters.     

Application of Hydrazino Dinitrophenyl-Amino Acids as Chiral Derivatizing Reagents for Liquid Chromatographic Enantioresolution of Carbonyl Compounds

A new series of chiral derivatizing reagents (CDRs) consisting of five hydrazino dinitrophenyl (HDNP)-amino acids (CDR 1?C5) was prepared by a two-step synthesis procedure starting from 1,5-difluoro-2,4-dinitrobenzene (DFDNB). In the first step, five fluoro-dinitrophenyl (FDNP)-reagents, namely FDNP-l-Leu, FDNP-l-Val, FDNP-l-Phe, FDNP-l-Ala and FDNP-d-Phg were synthesized by substituting one of the fluorine atoms in DFDNB moiety with amino acids l-Leu, l-Val, l-Phe, l-Ala and d-Phg, respectively. In the following step, the remaining fluorine atom of the FDNP reagents was substituted with hydrazine hydrate to obtain five HDNP reagents (i.e. CDR 1?C5; HDNP-l-Leu, HDNP-l-Val, HDNP-l-Phe, HDNP-l-Ala and HDNP-d-Phg). These five CDRs were used for synthesis of diastereomers of six racemic carbonyl compounds which were resolved by high-performance liquid chromatography using C18 column and gradient eluting mixture of acetonitrile or methanol with triethylammonium phosphate buffer with UV detection at 348 nm. Microwave irradiation was used for synthesis of both the CDRs and the diastereomers. The newly synthesized CDRs were observed to be superior in comparison to their counterparts having amino acid amides as chiral auxiliaries in terms of cost effectiveness and providing better resolution of diastereomers. The method was validated for limit of detection, linearity, accuracy and precision.     

pH-dependent complex formation of amino acids with β-cyclodextrin and quaternary ammonium β-cyclodextrin

Stability constants for the complexes of anionic, neutral (zwitterionic) and protonated forms of l- and d-enantiomers of eight amino acids with β-cyclodextrin and the positively charged quaternary ammonium β-cyclodextrin (QA-β-CD, DS?=?3.6?±?0.3) have been determined by spectrophotometric and pH-potentiometric methods. The highest stability constants have been obtained for the aromatic amino acids phenylalanine, tyrosine and tryptophan. Except the dianion of tyrosine and QA-β-CD, values for the anions in the range of 80–120 have been found, the stability constants for the zwitterionic forms are much smaller and complex formation is negligible with the protonated species. In the case of the other amino acids the differences are less pronounced. The results are interpreted in terms of hydrogen bonding, steric effects and electrostatic interactions between the amino acid moiety and the rims of the cyclodextrins, in addition to the inclusion of the side chain, and are supported by ¹H and ¹³C NMR investigations on the systems containing l-phenylalanine and l-tyrosine. The differences between the complex formation constants of the l- and d-enantiomers do not exceed the limits of experimental error in most cases.     

Study of the interaction between ethanol and natural amino acids containing ionic side groups in water at T = 298.15 K

The enthalpies of solution of l-α-aspartic acid, l-α-glutamic acid, l-α-arginine, l-α-lysine, and l-α-histidine have been measured in aqueous ethanol solutions at 298.15 K. From the obtained experimental results, the standard enthalpies of solution of amino acids in water–ethanol solutions have been determined. These data were used to calculate the heterogeneous enthalpic pair interaction coefficients based on McMillan–Mayer’s formalism. These values were interpreted in the terms of the ionic or no polar effect of the side chains of l-α-amino acids on their interactions with a molecule of ethanol in water.     

Effect of Cofactor Folate on the Growth of Corynebacterium glutamicum SYPS-062 and l-Serine Accumulation

The direct fermentative production of l-serine from sugar has attracted increasing attention. Corynebacterium glutamicum SYPS-062 can directly convert sugar to l-serine. In this study, the effects of exogenous and endogenous regulation of cofactor folate on C. glutamicum SYPS-062 growth and l-serine accumulation were investigated. For exogenous regulation, the inhibitor (sulfamethoxazole) or precursor (p-aminobenzoate) of folate biosynthesis was added to the medium, respectively. For endogenous regulation, the gene (pabAB) that encodes the key enzyme of folate biosynthesis was knocked out or overexpressed to obtain the recombinant C. glutamicum SYPS-062 ΔpabAB and SYPS-062(pJC-tac-pabAB), respectively. The results indicated that decreased levels of cofactor folate supported l-serine accumulation, whereas increased levels of cofactor folate aided in cell growth of C. glutamicum SYPS-062. Thus, this study not only elucidated the role of folate in C. glutamicum SYPS-062 growth and l-serine accumulation, but also provided a novel and convenient approach to regulate folate biosynthesis in C. glutamicum.     

Gas-phase basicities of serine and dipeptides of serine and glycine

The gas-phase basicities of serine and dipeptides containing amino acid residues of serine and glycine were determined by proton transfer reactions in a Fourier transform ion cyclotron resonance mass spectrometer. The gas-phase basicity (GB) of L-serine was found to be 205.9 kcal/mol, with addition of a hydroxymethyl group (?CH₂OH) increasing the basicity by 4.5 kcal/mol relative to the simplest amino acid glycine (GB = 201.4 kcal/mol). This is attributed to a combination of intramolecular hydrogen bonding, induction, and symmetry effects. For the dipeptides, addition of a hydroxymethyl group does not result in a large increase in basicity relative to the basicity of glycylglycine (GB = 208.0 kcal/mol). The gas-phase basicities determined for glycyl-l-serine, l-serylglycine, and l-sery-l-serine are 209.3,210.6, and 210.9 kcal/mol, respectively. In comparison to glycylglycine, addition of the hydroxymethyl group at the N terminus has a greater impact on basicity than its placement at the C terminus. These data suggest that the protonation site for these dipeptides is the N-terminal amino nitrogen.     

Solid state radiolysis of non-proteinaceous amino acids in vacuum: astrochemical implications

The analysis of the amino acids present in Murchison meteorite and in other carbonaceous chondrites has revealed the presence of 66 different amino acids. Only eight of these 66 amino acids are proteinaceous amino acids used by the present terrestrial biochemistry in protein synthesis, the other 58 amino acids are somewhat “rare” or unusual or even “unknown” for the current terrestrial biochemistry. For this reason in the present work a series of “uncommon” non-proteinaceous amino acids, namely, l-2-aminobutyric acid, R(?)-2-aminobutyric acid, 2-aminoisobutyric acid (or α-aminoisobutyric acid), l-norleucine, l-norvaline, l-β-leucine, l-β-homoalanine, l-β-homoglutamic acid, S(?)-α-methylvaline and dl-3-aminoisobutyric acid were radiolyzed in vacuum at 3.2 MGy a dose equivalent to that emitted in 1.05 × 10⁹ years from the radionuclide decay in the bulk of asteroids or comets. The residual amount of each amino acid under study remained after radiolysis was determined by differential scanning calorimetry in comparison to pristine samples. For optically active amino acids, the residual amount of each amino acid remained after radiolysis was also determined by optical rotatory dispersion spectroscopy and by polarimetry. With these analytical techniques it was possible to measure also the degree of radioracemization undergone by each amino acid after radiolysis. It was found that the non-proteinaceous amino acids in general do not show a higher radiation and radioracemization resistance in comparison to the common 20 proteinaceous amino acids studied previously. The unique exception is represented by α-aminoisobutyric acid which shows an extraordinary resistance to radiolysis since 96.6 % is recovered unchanged after 3.2 MGy. Curiously α-aminoisobutyric acid is the most abundant amino acid found in carbonaceous chondrites. In Murchison meteorite α-aminoisobutyric acid represents more than 20 % of the total 66 amino acids found in this meteorite.     

Protonation Equilibria of Some Selected α-Amino Acids in DMSO–Water Mixture and Their Cu(II)-Complexes

The protonation constants of some α-amino acids (glycine (Gly), l-alanine (Ala), l-valine (Val), l-serine (Ser), l-leucine (Leu) and l-isoleucine (Ile)) were studied in water and DMSO–water solution mixtures containing 30, 50 and 70 vol-% DMSO; in addition the complex formation equilibria of their copper(II) complexes were studied by potentiometric technique using a combined pH electrode system calibrated in concentration units of the hydrogen ion at 25 ± 0.1 °C under a nitrogen atmosphere, and at an ionic strength of 0.10 mol·dm^?3 NaNO₃. The protonation constants and the overall stability constants of copper(II) complexes were influenced by changes in solvent composition, and their variations are discussed in terms of solvent and structural properties.     

d- and l-amino acids in Antarctic lakes: assessment of a very sensitive HPLC-MS method

Amino acids represent a fraction of organic matter in marine and freshwater ecosystems, and a source of carbon, nitrogen and energy. l-Amino acids are the most common enantiomers in nature because these chiral forms are used during the biosynthesis of proteins and peptide. To the contrary, the occurrence of d-amino acids is usually linked to the presence of bacteria. We investigated the distribution of l- and d-amino acids in the lacustrine environment of Terra Nova Bay, Antarctica, in order to define their natural composition in this area and to individuate a possible relationship with primary production. A simultaneous chromatographic separation of 40 l- and d-amino acids was performed using a chiral stationary phase based on teicoplainin aglycone (chirobiotic tag). The chromatographic separation was coupled to two different mass spectrometers—an LTQ-Orbitrap XL (Thermo Fisher Scientific) and an API 4000 (ABSciex)—in order to investigate their quantitative performance. High-performance liquid chromatography coupled with mass spectrometry methods were evaluated through the estimation of their linear ranges, repeatability, accuracy and detection and quantification limits. The high-resolution mass spectrometer LTQ-Orbitrap XL presented detection limits between 0.4 and 7 μg?l ^?1, while the triple quadrupole mass spectrometer API 4000 achieved the best detection limits reported in the literature for the quantification of amino acids (between 4 and 200 ng?l ^?1). The most sensitive method, HPLC-API 4000, was applied to lake water samples. Figure

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Specific features of the reaction of l-cysteine with pyridoxal and N-pyridoxylidene-β-alanine

The mechanisms of condensation of l-cysteine, l-methionine, and l-serine with pyridoxal and of transaldimination of N-pyridoxylidene-??-alanine with l-cysteine were studied by the kinetic method. Unlike methionine and serine, the condensation of cysteine with pyridoxal and transaldimination with Npyridoxylidene-??-alanine involves intermediate formation of stable product having a thiazolidine ring. Its structure was determined by elemental analysis, UV, and IR spectroscopy, and quantum-chemical calculations. The thiazolidine fragment in the pyridoxal condensation product with l-cysteine is turned through an angle of ??90° with respect to the pyridine ring plane due to mutual repulsion of the negatively charged oxygen atom in the ortho position of the pyridine ring and sulfur and nitrogen atoms in the thiazolidine ring.     

The pivotal role of copper(II) in the enantiorecognition of tryptophan and histidine by gold nanoparticles

Stereoselective amino acid analysis has increasingly moved into the scope of interest of the scientific community. In this work, we report a study on the chiral recognition of d,l-Trp and d,l-His using l-Cys-capped gold nanoparticles (AuNPs) and copper(II) ion. In the l-Cys-capped AuNPs, the thiol group of the amino acid interacts with AuNPs through the formation of Au–S bond, whereas the α-amino and α-carboxyl groups of the surface-confined cysteine can coordinate the copper(II) ion, which in turn, binds the l- or d-amino acid present in solution forming diastereoisomeric complexes. The resulting systems have been characterized by UV–Vis spectra and dynamic light scattering measurements, obtaining different results for l- and d-Trp, as well as for l- and d-His. The knowledge of the solution equilibria of the investigated systems allowed us to accurately calculate in advance the concentrations of the species present in solution and to optimize the system performances, highlighting the pivotal role of copper(II) ion in the enantiodiscrimination processes.     

Thermodynamic and structural aspects of the interaction of l-histidine with urea and dimethylformamide in water

The solubility of l-histidine in water and aqueous solutions of dimethylformamide (DMF) at 25°C was determined. The thermal effects of solution of l-histidine in aqueous solutions of urea and DMF were measured. The standard enthalpies, free energies, and entropies of solution and transfer of the amino acid from water to aqueous solutions of amides were calculated. It was shown that the interaction of l-histidine with urea is attractive, and that with DMF, repulsive, with the change in the free energy determined by the enthalpy term in both cases. The enthalpy-entropy compensation taking place to a certain extent in the interaction of l-histidine and l-phenylalanine with amide was revealed. This effect is the most pronounced in the interaction of predominantly hydrophobic DMF and l-phenylalanine.     

Improved synthesis of rupintrivir

An improved synthesis of rupintrivir (AG7088) was accomplished using three amino acids (L-glutamic acid, D-4-fluorophenylalanine, and L-valine) as the building blocks. The key fragment ketomethylene dipeptide isostere was constructed with the valine derivative and phenylpropionic acid derivative, followed by coupling with a lactam derivative and an isoxazole acid chloride to provide AG7088 totally in eight steps.     

Volumetric and Viscometric Analyses for l-Glutamic Acid in NaCl Aqueous Solutions at Different Temperatures

The physico-chemical property data for l-glutamic acid in aqueous NaCl solutions were obtained at 0, 0.5, 1.0 and 2.0 mol·kg^?1 NaCl and amino acid molalities from 0 to 0.0669 mol·kg^?1 between 293.15 and 323.15 K. The influence of NaCl addition on the volumetric and viscometric properties of the amino acid has been studied. From the experimental densities, the apparent molar volumes and transfer volumes of l-glutamic acid in aqueous electrolyte solutions have been calculated. The viscosity data in the studied domain of amino acid molalities have led to the evaluation of the Falkenhagen and Jones–Dole viscosity coefficients of l-glutamic acid in NaCl aqueous solutions. The results have been discussed in terms of interactions occurring in the systems.     

Enhancing Production of l-Serine by Increasing the glyA Gene Expression in Methylobacterium sp. MB200

Microbial fermentation using methylotrophic bacteria is one of the most promising methods for l-serine production. Here we describe the metabolic engineering of a Methylobacterium strain to increase the production of l-serine. The glyA gene, encoding serine hydroxymethyltransferase (SHMT), was isolated from the genomic DNA of Methylobacterium sp. MB200, using a DNA fragment encoding Methylobacterium extorquens AM1 SHMT as a probe, and inserted into the vector pLAFR3. The resulting construct was transformed into Methylobacterium sp. MB200 using triparental mating. The genetic-engineered strain, designated as Methylobacterium sp. MB202, was shown to produce 11.4?±?0.6 mg/ml serine in resting cell reactions from 30 mg/ml wet cells, 20 mg/ml glycine, and 70 mg/ml methanol in 2 days, representing a 4.4-fold increase from that of the wild strain. The results demonstrated the potential for improving l-serine production by manipulating the glyA in bacteria and should facilitate the production of l-serine using Methylobacterium sp. strains.     

The yjjN of E. coli codes for an l-galactonate dehydrogenase and can be used for quantification of l-galactonate and l-gulonate

Escherichia coli is able to utilize l-galactonate as a sole carbon source. A metabolic pathway for l-galactonate catabolism is described in E. coli, and it is known to be interconnected with d-galacturonate metabolism. The corresponding gene encoding the first enzyme in the l-galactonate pathway, l-galactonate-5-dehydrogenase, was suggested to be yjjN. However, l-galactonate dehydrogenase activity was never demonstrated with the yjjN gene product. Here, we show that YjjN is indeed an l-galactonate dehydrogenase having activity also for l-gulonate. The K _m and k _cat for l-galactonate were 19.5?±?0.6 mM and 0.51?±?0.03 s^?1, respectively. In addition, YjjN was applied for a quantitative detection of the both of these substances in a coupled assay. The detection limits for l-galactonate and l-gulonate were 1.65 and 10 μM, respectively.