L-Phenylalanine-d5
(Synonyms: L-苯丙氨酸-d5) 目录号 : GC63982
L-Phenylalanine-d5 是 L-Phenylalanine 的氘代物。L-Phenylalanine ((S)-2-Amino-3-phenylpropionic acid) 是分离自大肠杆菌的必需氨基酸。L-Phenylalanine 是一种电压依赖性 α2δ 亚基 Ca2+ 通道拮抗剂，Ki 为 980 nM。L-Phenylalanine 是 NMDARs (KB 573 μM) 和非 NMDARs 的甘氨酸和谷氨酸结合位点的竞争性拮抗剂。L-Phenylalanine 广泛用于食品香料和药品的生产中。
Cas No.:56253-90-8
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
L-Phenylalanine-d5 is the deuterium labeled L-Phenylalanine. L-Phenylalanine ((S)-2-Amino-3-phenylpropionic acid) is an essential amino acid isolated from Escherichia coli. L-Phenylalanine is a α2δ subunit of voltage-dependent Ca+ channels antagonist with a Ki of 980 nM. L-phenylalanine is a competitive antagonist for the glycine- and glutamate-binding sites of N-methyl-D-aspartate receptors (NMDARs) (KB of 573 μM ) and non-NMDARs, respectively. L-Phenylalanine is widely used in the production of food flavors and pharmaceuticals[1][2][3][4].
Stable heavy isotopes of hydrogen, carbon, and other elements have been incorporated into drug molecules, largely as tracers for quantitation during the drug development process. Deuteration has gained attention because of its potential to affect the pharmacokinetic and metabolic profiles of drugs[1].
[1]. Russak EM, et al. Impact of Deuterium Substitution on the Pharmacokinetics of Pharmaceuticals. Ann Pharmacother. 2019;53(2):211-216.
| Cas No. | 56253-90-8 | SDF | Download SDF |
| 别名 | L-苯丙氨酸-d5 | ||
| 分子式 | C9H6D5NO2 | 分子量 | 170.22 |
| 溶解度 | 储存条件 | Store at -20°C, protect from light | |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 5.8748 mL | 29.3738 mL | 58.7475 mL |
| 5 mM | 1.175 mL | 5.8748 mL | 11.7495 mL |
| 10 mM | 0.5875 mL | 2.9374 mL | 5.8748 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Characterization of enzyme-bound ligand dynamics by solid-state NMR in the presence of ligand exchange: L-phenylalanine on carboxypeptidase A
Biophys J 1995 Jan;68(1):303-11.PMID:7711255DOI:10.1016/S0006-3495(95)80188-8.
Deuterium NMR spectra were obtained for L-Phenylalanine-d5, deuterated on the phenyl ring, in cross-linked polycrystalline samples of carboxypeptidase A containing different amounts of water. The deuterium powder pattern line shapes are simulated by extension of the theory to include both a local reorientational motion of the bound L-phenylalanine phenyl ring and exchange of the L-phenylalanine with an intracrystalline isotropic environment. The spectral simulations are consistent with the phenyl ring of the phenylalanine executing pi-flips in the bound environment at rates that vary from 3 x 10(4) Hz at 6% water content to 1 x 10(5) Hz at 21% water content. At all water contents studied, the ligand exchanges with an essentially isotropic environment in the crystal with a rate constant of approximately 2.5 x 10(-3) Hz. Although the dissociation constant for the L-phenylalanine is only 18 mM, the spectral simulations that reproduce the experimental line shape well do not require significant wobble of the phenyl ring rotation axis, which is consistent with the binding interactions identified by x-ray crystallography.
In vivo studies of the phenylalanine-4-hydroxylase system in hyperphenylalaninemics and phenylketonurics
Helv Paediatr Acta 1978 Feb;32(6):461-9.PMID:632110doi
An in vivo determination of the phenylalanine-4-hydroxylase (E. C. 1.14.16.1) activity is described. Subjects were loaded wit deuterated L-Phenylalanine-d5 (200 mg/kg), and the deuterated tyrosine and deuterated phenylalanine in plasma was analyzed using mass fragmentography. Six phenylketonurics (PKU), four hyperphenylalaninemics and two healthy controls were investigated. This method allowed a specific differentiation between PKU's, hyperphenylalaninemics and health controls. The remaining enzyme activity in hyperphenylalaninemics and in PKU patients can be estimated with relatively high accuracy. The hyperphenylalaninemic patients showed 7--17% of the phenylalanine-4-hydroxylase activity found in the two control persons. The PKU patients under diet showed approximately 2--3% of the activity found in the control group. In the PKU patients, loaded while showing high phenylalanine blood concentrations, no remaining activity could be measured. The logarithm of phenylalanine-d5 over tyrosine-d4 in plasma 1 h after loading gives the best differentiation. One single plasma sample of approximately 0.5 ml is sufficient.
Quantitation of deuterated and non-deuterated phenylalanine and tyrosine in human plasma using the selective ion monitoring method with combined gas chromatography-mass spectrometry. Application to the in vivo measurement of phenylalanine-4-monooxygenase activity
J Chromatogr 1977 Nov 11;142:523-31.PMID:914934DOI:10.1016/s0021-9673(01)92065-5.
A specific method is described for the quantitative analysis of deuterated and non-deuterated phenylalanine and tyrosine in human plasma by gas chromatography-mass spectrometry using selective ion monitoring. From the several derivatives investigated, the N- or N,O-trifluoroacetyl methyl esters were found to be the most suitable for our purposes. DL-Phenylalanine-4-d1 and L-tyrosine-d7 were used as internal standards. The sensitivity of this method permits the measurement of amounts as small as ca. 2.5 ng/ml in plasma for both phenylalanine and tyrosine. The coefficients of variation were found to be ca. 1.6% (n = 12) for phenylalanine and 3.0% (n = 12) for tyrosine. Using this method, an in vivo determination of phenylalanine-4-monooxygenase activity in humans is possible by loading the subjects with deuterated L-Phenylalanine-d5 (accepted as substrate by phenylalanine-4-monooxygenase E.C. 1.14.16.1) and the subsequent measuring of deuterated L-tyrosine-d4 formed and residual L-Phenylalanine-d5.