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At least 163 records · Page 9Linked to original sources
PubMed2004

Adsorption of aspartic acid on kaolinite.

The interaction of aspartic acid with kaolinite was studied by potentiometric titrations and by adsorption measurements both at constant aspartate concentration (but varying pH) and at a constant pH of 5.5. The temperature was 25 degrees C, and the ionic medium 5 mM KNO3. Aspartic acid dissociation constants estimated from titrations agreed with those from the literature. The adsorption of aspartic acid to kaolinite was weak and varied only slightly with pH; 10-18% of 100 microM aspartic acid adsorbed to kaolinite at 100 m(2)L(-1) between pH 3 and 10. Data from the titrations and adsorption experiments were fitted closely by an extended constant-capacitance surface complexation model, in which monodentate outer-sphere complexes formed between deprotonated aspartic acid molecules and protonated sites on the variable-charge edges of the kaolinite crystals. There appeared to be no adsorption to the permanently charged crystal faces.

Journal Article↗
PubMed1999

The taste of monosodium glutamate (MSG), L-aspartic acid, and N-methyl-D-aspartate (NMDA) in rats: are NMDA receptors involved in MSG taste?

Monosodium glutamate (MSG) is believed to elicit a unique taste perception known as umami. We have used conditioned taste aversion assays in rats to compare taste responses elicited by the glutamate receptor agonists MSG, L-aspartic acid (L-Asp), and N-methyl-D-aspartate (NMDA), and to determine if these compounds share a common taste quality. This information could shed new light upon the receptor mechanisms of glutamate taste transduction. Taste aversions to either MSG, L-Asp or NMDA were produced by injecting rats with LiCl after they had ingested one of these stimuli. Subsequently, rats were tested to determine whether they would ingest any of the above compounds. The results clearly show that a conditioned aversion to MSG generalized to L-Asp in a dose-dependent manner. Conversely, rats conditioned to avoid L-Asp also avoided MSG. Conditioned aversions to MSG or L-Asp generalized to sucrose when amiloride was included in all solutions. Importantly, aversions to MSG or L-Asp did not generalize to NMDA, NaCl or KCl, and aversions to NMDA did not generalize to MSG, L-Asp, sucrose or KCl. These data indicate that rats perceive MSG and L-Asp as similar tastes, whereas NMDA, NaCl and KCl elicit other tastes. The results do not support a dominant role for the NMDA subtype of glutamate receptors in taste transduction for MSG (i.e. umami) in rats.

Animals↗
PubMed2001

Novel amino acid substitutional mutation, tyrosine-739-aspartic acid, in the androgen receptor gene in complete androgen insensitivity syndrome.

Androgen insensitivity syndrome (AIS) is an X-linked recessive disorder. The molecular mechanism of AIS is reduction or absence of androgen signalling caused by androgen receptor (AR) malfunction or absence. The phenotype of AIS varies from a complete female phenotype (complete AIS, CAIS) to male genitalia with mild hypospadias (partial AIS, PAIS). In the current study, we characterize a novel point mutation in the ligand binding domain of the AR gene in a 50-year-old Japanese CAIS patient. Sequence analysis showed a single point mutation at nucleotide 3359 (Genbank, NM 000044), T to C, in exon E in the AR gene. This mutation led to the conversion of codon 739 tyrosine into aspartic acid in the ligand binding domain. No specific androgen binding was detected in genital fibroblasts isolated from the patient. Transcriptional activating activity of the mutant AR was examined by transient DNA transfection into COS-1 cells. Wild-type AR successfully activated androgen inducible MMTV promoter dose-dependently. In contrast, the mutant AR did not activate MMTV promoter. Thus, we demonstrated the molecular characteristics of the novel point mutation in the ligand binding domain of the AR gene associated with CAIS. This information will provide a further understanding of the structure and function of the AR gene.

Amino Acid Substitution↗
PubMed2003

Synthesis of various 3-substituted 1,2,4-oxadiazole-containing chiral beta 3- and alpha-amino acids from Fmoc-protected aspartic acid.

Various 3-substituted chiral 1,2,4-oxadiazole-containing Fmoc-beta(3)- and -alpha-amino acids were synthesized from Fmoc-(l or d)-Asp(OtBu)-OH and Fmoc-l-Asp-OtBu, respectively, in three steps (i.e., condensation of an aspartyl derivative with differentially substituted amidoximes, formation of the 1,2,4-oxadiazole, and cleavage of the tert-butyl ester). These compounds represent new series of nonnatural amino acids, which could be used in combinatorial synthesis. A simple protocol has been developed to generate the 1,2,4-oxadiazole ring. Indeed, common methods resulted in cleavage of the Fmoc group or required long reaction times. We found that sodium acetate in refluxing ethanol/water (86 degrees C) was a convenient and efficient catalyst to promote conversion of Fmoc-amino acyl amidoximes to 1,2,4-oxadiazoles, and this procedure proved to be compatible with Fmoc protection. It is shown that these compounds can be prepared without significant loss of enantiomerical purity. Furthermore, the alkaline conditions used to cleave the Fmoc protecting group from these compounds did not induce epimerization of their chiral center.

Amino Acids↗
PubMedDate not supplied

Biochemical and molecular characterization of poly(aspartic acid) hydrolase-2 from sphingomonas sp. KT-1.

Poly(aspartic acid) (PAA) hydrolase-2 was purified from crude soluble cellular extracts of Sphingomonas sp. KT-1 (JCM10459) and characterized to elucidate the mechanism of alpha,beta-poly(d,l-aspartic acid) (tPAA) biodegradation. The molecular mass of PAA hydrolase-2 was 42 kDa, and the isoelectric point was 9.6. The optimum values of pH and temperature for the hydrolysis of alpha-di(l-aspartic acid) by PAA hydrolase-2 were 7.0 and 55 degrees C, respectively. The effect of inhibitors on the hydrolysis of alpha-di(l-aspartic acid) showed that the activity of PAA hydrolase-2 was significantly inhibited by EDTA. Thermally synthesized tPAA was hydrolyzed in the presence of two enzymes, PAA hydrolase-1 and PAA hydrolase-2, to generate aspartic acid. The PAA hydrolase-2 was capable of hydrolyzing alpha-poly(l-aspartic acid) of high molecular weights but had limited activity for tPAA. These results lead us to propose the following mechanism. First, PAA hydrolase-1 hydrolyzes tPAA to yield oligo(aspartic acid) via an endo-mode cleavage, and subsequently, PAA hydrolase-2 hydrolyzes the resultant oligo(aspartic acid) to yield aspartic acid. Analysis of hydrolyzed products from alpha- and beta-penta(l-aspartic acid) revealed that PAA hydrolase-2 catalyzed the exo-mode hydrolysis of alpha- and beta-penta (l-aspartic acid). The gene encoding PAA hydrolase-2 from Sphingomonas sp. KT-1 was cloned, and genetic analysis showed that the deduced amino acid sequence of PAA hydrolase-2 is similar to a putative peptidase, which belongs to the M20/M25/M40 family of proteins, from Caulobacter crescentus CB15.

Amino Acid Sequence↗
PubMed1994

Analysis of aspartic acid and asparagine metabolism in Xenopus laevis oocytes using a simple and sensitive HPLC method.

The amino acids in methanol-soluble extracts of Xenopus oocytes were measured using a method involving precolumn derivatization with phenylisothiocyanate and reverse phase HPLC of the derivatized amino acids. This technique allows the estimation of asparagine and glutamine pools in oocytes, estimated as 70 and 283 pmoles per oocyte, respectively. The pool sizes of the other amino acids were similar to previously reported results obtained using conventional ion exchange chromatography and postcolumn derivatization with ninhydrin. The advantages of the method developed here include picomolar sensitivity and the enhanced resolution of asparagine and glutamine from other amino acids. The kinetics of aspartic acid and asparagine utilization were monitored following microinjection of oocytes with [3H]aspartic acid and [14C]asparagine. The aspartic acid pool turned over rapidly with a half-time of < 30 min. The asparagine pool was metabolized much more slowly and appeared to be utilized almost completely for protein synthesis. The absolute rate of protein synthesis in oocytes was calculated from the incorporation data and chemical pool measurements as approximately 25 ng/hr-oocyte. The methodology developed here may be useful in experimental situations involving limited amounts of biological material.

Amino Acids↗
PubMed2006

Synthesis and characterization of poly(L-lactic acid-co-ethylene oxide-co-aspartic acid) and its interaction with cells.

Multiblock terpolymer of poly(L-lactic acid)/poly(ethylene oxide)/poly(L-aspartic acid), (PLLA/PEO/PAsp) was synthesized by ring opening polymerization of beta -benzyl L-aspartate N-carboxyanhydride, Asp(OBzl)-NCA with alpha-omega -hydroxy terminated triblock PLLA/PEO/PLLA copolymer. The resulting multiblock terpolymer was characterized by several techniques including Fourier transform infrared spectroscopy and differential scanning calorimetry.(1)H nuclear magnetic resonance spectra indicated the molar ratio of PLLA/PEO/PAsp (OBzl) to be 86/10/4. Thermal gravimetric analysis and environmental scanning electron microscopy data showed that PLLA/PEO/PAsp had crystalline and brittle structure. In order to improve its mechanical and physical properties, the terpolymer was blended with high molecular weight poly(L-lactic-co-glycolic acid) copolymer, PLGA(85/15) (M(w): 95000 gmol(-1)) in 25/75 and 50/50 mole ratios. The hydrolytical degradation properties of these polymers were studied. Degradation experiments were performed during a 48-day period in pH:7.4 phosphate-buffered saline (PBS) at 37 degrees C. The observed molecular weight losses were 91% and 67% for the 25/75 and 50/50 mixtures, respectively. In vitro attachment and growth of L929 mouse fibroblasts on these biopolymers were also investigated. Cell growth experiments indicated that the copolymer blend allowed the attachment and growth of cells.

Animals↗
PubMed1994

Herpes simplex virus ribonucleotide reductase subunit association inhibitors: the effect and conformation of beta-alkylated aspartic acid derivatives.

Incorporating beta-alkylated aspartic acid derivatives into herpes simplex virus ribonucleotide reductase subunit association inhibitors can improve inhibitor potency up to 50 times over the corresponding inhibitors containing an unsubstituted aspartic acid. A combination of NMR studies, conformational analysis, and molecular mechanics calculations suggests that the beta-alkyl group improves inhibitor potency by favoring the bioactive conformation of the critical aspartic acid carboxyl group. Further support for this hypothesis is provided by a potent conformationally restricted aspartic acid derivative in which the carboxyl group is locked in the putative bioactive conformation.

Alkylation↗
PubMed1995

Antinociceptive effect of D-aspartic acid in mice.

The effects of D- and L-aspartic acids on the nociceptive tail flick reflex in mice were investigated. D-Aspartic acid (115-230 mg/kg, IP) was found to increase tail flick latency significantly. Naloxone (0.1 mg/kg) abolished the analgesic effect of D-aspartic acid (115 mg/kg). Morphine and D-aspartic acid, when combined at their nonanalgesic doses, led to significant analgesia. It may be concluded that the opioid system is involved in the antinociceptive effect of D-aspartic acid. Both morphine and D-aspartic acid were previously reported to inhibit L-aspartic acid production via blockade of L-asparaginase. L-Aspartic acid, which was ineffective alone, significantly inhibited the antinociceptive effects of both D-aspartic acid and morphine.

Analgesics↗
PubMed2004

Control over the crystal phase, shape, size and aggregation of calcium carbonate via a L-aspartic acid inducing process.

The acidic amino acid, such as aspartic acid (l-Asp), and glutamic acid are the primary active molecules of the glycoprotein on the organic/inorganic interface of biomineralized tissue. In this study, aspartic acid was used as the organic template in inducing the nucleation and growth of calcium carbonate. With the analysis of X-ray diffraction we investigated the relationship between the l-Asp concentration and the precipitation phase crystal structure of calcium carbonate. SEM and TEM were employed in the analysis of the morphological characteristic of the precipitation and the aggregation of the nanoscale porous phase. In order to get the direct evidence of the interaction between Ca2+ and l-Asp, the technique of QCM was used in the investigation of the coordinate interaction of Ca2+/l-Asp. As the results have shown, l-Asp alone is adequate to switch the transformation between calcite and vaterite, and neither soluble organic additions nor metal ions are needed. Meanwhile, the morphology, size and aggregative way of the deposition are also mediated with change of l-Asp concentration. To interpret the cause of the hierarchic structure range from nanoscale to micron-scale and the formation of the porous spheres of vaterite, an assumption of limited-fusion was proposed from the view of the small biomolecules polarity that can control over the growth of the crystals and the aggregation of the micro crystals. The conclusion also provide a new material synthesize strategy.

Adsorption↗
PubMed1999

Carbonyl-carbonyl interactions stabilize the partially allowed Ramachandran conformations of asparagine and aspartic acid.

Asparagine and aspartate are known to adopt conformations in the left-handed alpha-helical region and other partially allowed regions of the Ramachandran plot more readily than any other non-glycyl amino acids. The reason for this preference has not been established. An examination of the local environments of asparagine and aspartic acid in protein structures with a resolution better than 1.5 A revealed that their side-chain carbonyls are frequently within 4 A of their own backbone carbonyl or the backbone carbonyl of the previous residue. Calculations using protein structures with a resolution better than 1.8 A reveal that this close contact occurs in more than 80% of cases. This carbonyl-carbonyl interaction offers an energetic sabilization for the partially allowed conformations of asparagine and aspartic acid with respect to all other non-glycyl amino acids. The non-covalent attractive interactions between the dipoles of two carbonyls has recently been calculated to have an energy comparable to that of a hydrogen bond. The preponderance of asparagine in the left-handed alpha-helical region, and in general of aspartic acid and asparagine in the partially allowed regions of the Ramachandran plot, may be a consequence of this carbonyl-carbonyl stacking interaction.

Amino Acids↗
PubMed1993

Enhanced recovery and purification of Aspergillus glucoamylase from Saccharomyces cerevisiae by the addition of poly(aspartic acid) tails.

Poly(aspartic acid) tails of different lengths were fused to the glucoamylase (GA) of Aspergillus awamori by genetic engineering techniques. Tails consisting of 5, 7, and 10 aspartate residues were fused to the N-terminus of the full-length mature GA (aa 1-616) downstream from the intact leader peptide to produce fusion proteins designated GAND5, GAND7, and GAND10, respectively. Three fusion proteins with C-terminal tails were also constructed, designated GACD0, GACD5, and GACD10 (0, 5, and 10 aspartate residues, respectively). For the C-terminal fusion proteins, the tails were fused to a catalytically active but truncated form of GA (aa 1-484). All of the charged tails had the general sequence Met-Ala-Aspn-Tyr, where n = 0, 5, 7, or 10. The modified genes were expressed in the yeast Saccharomyces cerevisiae and the proteins secreted into the culture medium. The enzymes were subsequently purified by affinity chromatography. The specific activity of each purified enzyme was found to be comparable to the wild-type enzyme. The C-terminal tails did not interfere with expression, whereas decreased extracellular glucoamylase activities corresponding to increased tail length were found for the N-terminal fusion proteins. Amino-terminal amino acid sequence analysis of the purified GAND proteins confirmed the authenticity of the amino termini of the modified proteins and showed that both the leader peptidase and KEX2 protease cleavages had occurred faithfully. The increased net negative charge of the GAND and GACD proteins was indicated by both nondenaturing PAGE and isoelectric focusing.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1995

Mutation of the aspartic acid residues of the GDD sequence motif of poliovirus RNA-dependent RNA polymerase results in enzymes with altered metal ion requirements for activity.

The poliovirus RNA-dependent RNA polymerase, 3Dpol, is known to share a region of sequence homology with all RNA polymerases centered at the GDD amino acid motif. The two aspartic acids have been postulated to be involved in the catalytic activity and metal ion coordination of the enzyme. To test this hypothesis, we have utilized oligonucleotide site-directed mutagenesis to generate defined mutations in the aspartic acids of the GDD motif of the 3Dpol gene. The codon for the first aspartate (3D-D-328 [D refers to the single amino acid change, and the number refers to its position in the polymerase]) was changed to that for glutamic acid, histidine, asparagine, or glutamine; the codons for both aspartic acids were simultaneously changed to those for glutamic acids; and the codon for the second aspartic acid (3D-D-329) was changed to that for glutamic acid or asparagine. The mutant enzymes were expressed in Escherichia coli, and the in vitro poly(U) polymerase activity was characterized. All of the mutant 3Dpol enzymes were enzymatically inactive in vitro when tested over a range of Mg2+ concentrations. However, when Mn2+ was substituted for Mg2+ in the in vitro assays, the mutant that substituted the second aspartic acid for asparagine (3D-N-329) was active. To further substantiate this finding, a series of different transition metal ions were substituted for Mg2+ in the poly(U) polymerase assay. The wild-type enzyme was active with all metals except Ca2+, while the 3D-N-329 mutant was active only when FeC6H7O5 was used in the reaction. To determine the effects of the mutations on poliovirus replication, the mutant 3Dpol genes were subcloned into an infectious cDNA of poliovirus. The cDNAs containing the mutant 3Dpol genes did not produce infectious virus when transfected into tissue culture cells under standard conditions. Because of the activity of the 3D-N-329 mutant in the presence of Fe2+ and Mn2+, transfections were also performed in the presence of the different metal ions. Surprisingly, the transfection of the cDNA containing the 3D-N-329 mutation resulted in the production of virus at a low frequency in the presence of FeSO4 or CoCl2. The virus derived from transfection in the presence of FeSO4 grew slowly, while the viruses recovered from transfection in CoCl2 grew at a rate which was similar to that of the wild-type poliovirus.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acid Sequence↗
PubMed1989

Exploration of phenyl-spaced 2-amino-(5-9)-phosphonoalkanoic acids as competitive N-methyl-D-aspartic acid antagonists.

To investigate the preferred spatial relationship of the distal phosphonic acid to the alpha-amino acid group of the established competitive N-methyl-D-aspartic acid (NMDA) antagonists APH (1) and APV (2), we have prepared a series of ortho-, meta-, and para-substituted (phosphonoalkyl)phenylglycine and -phenylalanine derivatives. With use of a [3H]CPP receptor binding assay, significant binding activity was observed to be critically dependent on both the position of substitution and length of alkyl spacing groups. Two compounds, 4-(phosphonomethyl)-phenylglycine (6, PD 129635) and 3-(phosphonomethyl)phenylalanine (15, PD 130527), displayed receptor-binding affinity comparable to that of APH. Like APH, these compounds were also effective in antagonizing both the proconvulsant and lethal action of NMDA-administered retrobulbar in the mouse. Data are also provided which compare directly the binding efficacy of these compounds against that disclosed recently for the related NMDA antagonist 18 (NPC 451). A preliminary comparison of the structures showing good receptor-binding affinity and in vivo antagonist activity suggests that the NMDA receptor prefers a "folded" rather than "extended" conformation.

Amino Acids↗
PubMed1992

Occurrence of free D-aspartic acid in marine macroalgae.

The biologically rare D-aspartic acid was found in extracts of marine macroalgae. DL-aspartic acid was isolated from the Phaeophyta, Hizikia fusiformis, by ion-exchange chromatography, and crystallized from aqueous ethanol. It was characterized by optical-rotatory-dispersion analysis and reversed-phase HPLC analysis. The crystal consisted of equal amounts of D and L isomers. The presence of free D-aspartic acid was verified in 15 species from among 20 species of marine macroalgae by the same method (HPLC). Generally, Phaeophyta contained a high concentration of D-aspartic acid in contrast with the low concentration in Phycophyta and Rhodophyta. Particularly in Costaria costata, Hizikia fusiformis and Sargassum yezoensis, belonging to Phaeophyta, D-aspartic acid was found in concentrations proportional to those of L-aspartic acid.

Aspartic Acid↗
PubMed2006

A physiological mechanism to regulate D-aspartic acid and NMDA levels in mammals revealed by D-aspartate oxidase deficient mice.

Free D-aspartic acid and NMDA are present in the mammalian central nervous system and endocrine glands at significant concentrations, but their physiological role is still matter of debate. The only enzyme known to metabolize in vitro selectively these D-amino acids is D-aspartate oxidase (DDO). To clarify the role in vivo of the enzyme, we generated mice with targeted deletion of Ddo gene by homologous recombination. Mutated animals showed increased amounts of both D-aspartic acid and NMDA in all tissues examined demonstrating a physiological role of DDO in the regulation of their endogenous levels.

Animals↗