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D-Aspartic acid

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D-Aspartic acid is a kind of non-essential amino acid found in food sources and dietary supplements. It is an endogenous NMDA receptor agonist and has similar activity to the L-isomer. It is also a non-metabolizable substrate for EAA uptake systems. It adjusts melatonin synthesis in the pineal gland. It may be used as a therapeutic agent in the treatment of schizophrenia-related symptoms.

Category

D-Amino Acids

Catalog number

BAT-008096

CAS number

1783-96-6

Molecular Formula

C4H7NO4

Molecular Weight

133.10

IUPAC Name

(2R)-2-aminobutanedioic acid

Synonyms

(-)-Aspartic Acid; (R)-Aspartic Acid; D-(-)-Aspartic Acid; 2-Aminobutanedioic Acid; NSC 97922; NSC97922; NSC-97922; (R)-(−)-Aminosuccinic acid; (R)-2-Aminosuccinic acid; D-Aminosuccinic acid

Appearance

White crystalline powder

Purity

97%

Density

1.514 g/cm3

Melting Point

> 300 °C

Boiling Point

264.1°C at 760 mmHg

Storage

Store at RT

Solubility

Soluble in Aqueous Acid

InChI

InChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m1/s1

InChI Key

CKLJMWTZIZZHCS-UWTATZPHSA-N

Canonical SMILES

C(C(C(=O)O)N)C(=O)O

D-Aspartic acid (D-Asp) is a naturally occurring amino acid that is an isomer of the more commonly known L-Aspartic acid. Unlike L-Aspartic acid, which plays a significant role in metabolic pathways and neurotransmission, D-Aspartic acid is less prevalent in nature but has been identified as having unique biological functions. It is primarily found in the central nervous system and various endocrine tissues. In the human body, D-Aspartic acid is involved in the synthesis and release of hormones, including luteinizing hormone (LH) and growth hormone (GH), which are crucial for reproductive health and growth processes. Due to its distinct properties, D-Aspartic acid has garnered attention for its potential applications in various industrial fields.

One key industrial application of D-Aspartic acid is in the pharmaceutical industry. Its role in hormone regulation has led to its use in developing supplements aimed at enhancing hormonal balance, particularly for conditions related to growth and reproductive health. For instance, D-Aspartic acid is utilized in products designed to boost testosterone levels in men, which can support muscle growth and overall vitality. Furthermore, its potential therapeutic effects are being explored for treating disorders related to hormone imbalances, making it a valuable component in drug formulation and health supplements.

Another significant application of D-Aspartic acid is in the agriculture sector. It is used as a component in animal feed additives to enhance growth and reproductive efficiency in livestock. By influencing the release of growth hormones, D-Aspartic acid helps improve the overall health and productivity of farm animals. This application is particularly relevant in maximizing the yield and quality of livestock products, such as meat and dairy, which are crucial for meeting the demands of the agricultural industry.

In the field of biotechnology, D-Aspartic acid is employed in enzyme engineering and protein synthesis. Its unique structural properties make it a useful tool for modifying enzyme activity and stability, which is essential for various biotechnological processes. For example, it can be used to optimize enzyme performance in industrial applications, such as biotransformations and chemical synthesis. Additionally, D-Aspartic acid is involved in developing new biocatalysts that can improve efficiency and sustainability in biotechnology.

Finally, D-Aspartic acid has applications in the cosmetic industry, where it is used in the formulation of skincare products. Its role in hormone regulation and cell signaling makes it beneficial for products targeting skin rejuvenation and anti-aging. By supporting cellular health and promoting the production of collagen, D-Aspartic acid helps improve skin texture and elasticity. This application highlights its versatility and potential in enhancing cosmetic formulations for better skin health and appearance.

1.Sodium-dependent D-aspartate 'binding' is not a measure of presynaptic neuronal uptake sites in an autoradiographic assay.

Greenamyre JT;Higgins DS;Young AB Brain Res. 1990 Mar 19;511(2):310-8.

The binding of D-[3H]aspartate to sections of rat brain was examined in an autoradiographic assay. Binding was entirely dependent on the presence of sodium ions, but not chloride ions, and was optimal at 2 degrees C. D-Aspartate bound rapidly, reached equilibrium within 20 min and remained stable for 45 min. The rate of dissociation was relatively rapid with a t1/2 of 56 s, but was not as fast as anticipated, perhaps because of some sequestration of ligand. Binding had a Kd of 6.8 +/- 1.2 microM and a Bmax of 49.4 +/- 8.6 pmol/mg protein. The high Bmax value may further indicate some sequestration of D-aspartate. L-Glutamate, unlabeled D-aspartate, and D,L-threo-hydroxyaspartate, a potent inhibitor of synaptosomal uptake, each competed for D-[3H]aspartate binding with IC50s of 7.0 +/- 4.3 microM, 5.4 +/- 1.5 microM, and 2.5 +/- 1.0 microM, respectively. N-methyl-D-aspartate (NMDA), quisqualate, and kainate had no affinity for this site. The regional distribution of D-aspartate binding sites was unique and did not conform to the distribution of neuronal uptake sites described by others. Striatal D-aspartate binding was unaffected by unilateral decortication or striatal quinolinic acid lesions.

2.Evidence for two mechanisms of amino acid osmolyte release from hippocampal slices.

Franco R;Torres-Márquez ME;Pasantes-Morales H Pflugers Arch. 2001 Aug;442(5):791-800.

A 30% decrease in osmolarity stimulated 3H-taurine, 3H-GABA and glutamate (followed as 3H-D-aspartate) efflux from rat hippocampal slices. 3H-taurine efflux was activated rapidly but inactivated slowly. It was decreased markedly by 100 microM 5-nitro-(3-phenylpropylamino)benzoic acid (NPPB) and 600 microM niflumic acid and inhibited strongly by tyrphostins AG18, AG879 and AG112 (25-100 microM), suggesting a tyrosine kinase-mediated mechanism. Hyposmolarity activated the mitogen-activated protein kinases (MAPK) extracellular-signal-related kinase-1/2 (ERK1/ERK2) and p38, but blockade of this reaction did not affect 3H-taurine efflux. Hyposmosis also activated phosphatidylinositide 3-kinase (PI3K) and its prevention by wortmannin (100 nM) essentially abolished 3H-taurine efflux. 3H-taurine efflux was insensitive to the protein kinase C (PKC) blocker chelerythrine (2.5 microM) or to cytochalasin E (3 microM). The release of 3H-GABA and 3H-D-aspartate occurred by a different mechanism, characterized by rapid activation and inactivation, insensitivity to NPPB, niflumic acid, tyrphostins or wortmannin. 3H-GABA and 3H-D-aspartate efflux was not due to external [NaCl] decrease, cytosolic Ca2+ increase or depolarization, or to reverse operation of the carrier.

3.Racemization of the Succinimide Intermediate Formed in Proteins and Peptides: A Computational Study of the Mechanism Catalyzed by Dihydrogen Phosphate Ion.

Takahashi O;Kirikoshi R;Manabe N Int J Mol Sci. 2016 Oct 10;17(10). pii: E1698.

In proteins and peptides, d-aspartic acid (d-Asp) and d-β-Asp residues can be spontaneously formed via racemization of the succinimide intermediate formed from l-Asp and l-asparagine (l-Asn) residues. These biologically uncommon amino acid residues are known to have relevance to aging and pathologies. Although nonenzymatic, the succinimide racemization will not occur without a catalyst at room or biological temperature. In the present study, we computationally investigated the mechanism of succinimide racemization catalyzed by dihydrogen phosphate ion, H₂PO₄;-;, by B3LYP/6-31+G(d,p) density functional theory calculations, using a model compound in which an aminosuccinyl (Asu) residue is capped with acetyl (Ace) and NCH₃ (Nme) groups on the N- and C-termini, respectively (Ace-Asu-Nme). It was shown that an H₂PO₄;-; ion can catalyze the enolization of the H;α;-C;α;-C=O portion of the Asu residue by acting as a proton-transfer mediator. The resulting complex between the enol form and H₂PO₄;-; corresponds to a very flat intermediate region on the potential energy surface lying between the initial reactant complex and its mirror-image geometry. The calculated activation barrier (18.8 kcal·mol;-1; after corrections for the zero-point energy and the Gibbs energy of hydration) for the enolization was consistent with the experimental activation energies of Asp racemization.