4-Azido-L-phenylalanine (p-Azidophenylalanine)
(Synonyms: 4-叠氮基-L-苯丙氨酸,p-Azidophenylalanine; p-Azido-L-phenylalanine) 目录号 : GC30007
4-叠氮基-L-苯丙氨酸 (p-Azidophenylalanine) 是一种非天然氨基酸，可用作局部蛋白质环境的有效振动报告分子。
Cas No.:33173-53-4
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
4-Azido-L-phenylalanine is an unnatural amino acid, which is used as an effective vibrational reporter of local protein environments.
In cell-free protein synthesis (CFPS) method, 0.9-1.7 mg/mL of modified soluble super-folder green fluorescent protein (sfGFP) containing either 4-Azido-L-phenylalanine or p-propargyloxy-l-phenylalanine (pPaF) accumulate in the CFPS solutions[1].
[1]. Albayrak C, et al. Cell-free co-production of an orthogonal transfer RNA activates efficient site-specific non-natural amino acid incorporation. Nucleic Acids Res. 2013 Jun;41(11):5949-63.
| Cas No. | 33173-53-4 | SDF | |
| 别名 | 4-叠氮基-L-苯丙氨酸,p-Azidophenylalanine; p-Azido-L-phenylalanine | ||
| Canonical SMILES | O=C(O)[C@@H](N)CC1=CC=C(N=[N+]=[N-])C=C1 | ||
| 分子式 | C9H10N4O2 | 分子量 | 206.2 |
| 溶解度 | Water : 6.2 mg/mL (30.07 mM; ultrasonic and adjust pH to 6 with HCl);DMSO : 6 mg/mL (29.10 mM; ultrasonic and adjust pH to 6 with HCl) | 储存条件 | Store at -20°C |
| 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。 |
||
| 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 | |||
 |
1 mg | 5 mg | 10 mg |
| 1 mM | 4.8497 mL | 24.2483 mL | 48.4966 mL |
| 5 mM | 0.9699 mL | 4.8497 mL | 9.6993 mL |
| 10 mM | 0.485 mL | 2.4248 mL | 4.8497 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。
Synthesis and Explosion Hazards of 4-Azido-L-phenylalanine
J Org Chem 2018 Apr 20;83(8):4525-4536.29577718 PMC6008159
A reliable, scalable, cost-effective, and chromatography-free synthesis of 4-Azido-L-phenylalanine beginning from l-phenylalanine is described. Investigations into the safety of the synthesis reveal that the Ullman-like Cu(I)-catalyzed azidation step does not represent a significant risk. The isolated 4-Azido-L-phenylalanine product, however, exhibits previously undocumented explosive characteristics.
Synthesis of p-amino-L-phenylalanine derivatives with protected p-amino group for preparation of p-azido-L-phenylalanine peptides
Int J Pept Protein Res 1980 Apr;15(4):323-30.7419359 10.1111/j.1399-3011.1980.tb02908.x
For the synthesis of p-Azidophenylalanine peptides, the p-amino group of p-amino-L-phenylalanine is protected with the Z- or Boc residue via the copper complex or by specific acylation at pH 4.6. The alpha-amino or alpha-carboxy group is blocked by a protecting group (Boc, Ddz, OMe respectively Z, Nps, Ddz), which can be removed selectively. The synthesis of nine derivatives of p-amino-L-phenylalanine for incorporation into the peptide chain is described. The p-amino-phenylalanine is converted to p-Azidophenylalanine without affecting disulfide bridges.
The Effects of p-Azidophenylalanine Incorporation on Protein Structure and Stability
J Chem Inf Model 2020 Oct 26;60(10):5117-5125.32966074 10.1021/acs.jcim.0c00725
Functionalization is often needed to harness the power of proteins for beneficial use but can cause losses to stability and/or activity. State of the art methods to limit these deleterious effects accomplish this by substituting an amino acid in the wild-type molecule into an unnatural amino acid, such as p-Azidophenylalanine (pAz), but selecting the residue for substitution a priori remains an elusive goal of protein engineering. The results of this work indicate that all-atom molecular dynamics simulation can be used to determine whether substituting pAz for a natural amino acid will be detrimental to experimentally determined protein stability. These results offer significant hope that local deviations from wild-type structure caused by pAz incorporation observed in simulations can be a predictive metric used to reduce the number of costly experiments that must be done to find active proteins upon substitution with pAz and subsequent functionalization.
Identifying and Modulating Accidental Fermi Resonance: 2D IR and DFT Study of 4-Azido-L-phenylalanine
J Phys Chem B 2018 Aug 30;122(34):8122-8133.30067030 10.1021/acs.jpcb.8b03887
Azido-modified aromatic amino acids have been used as powerful infrared probes for the site-specific detection of proteins because of their large transition dipole strengths. However, their complex absorption profiles hinder their wider application. The complicated absorption profile of 4-Azido-L-phenylalanine (pN3Phe) in isopropanol was identified and attributed to accidental Fermi resonances (FRs) by means of linear absorption and two-dimensional (2D) IR spectroscopies. The 2D IR results of pN3Phe in H2O and D2O further demonstrate that the FRs are distinctively influenced by the hydrogen-bonding environment. Under the influence of FRs, the 2D IR shape is distorted, indicating that pN3Phe is not a good candidate in spectral diffusion studies. A three-state model and first-principles calculations were used to analyze unperturbed energy levels, unveiling the FRs between the azide asymmetric stretching band and two combination bands. Furthermore, the anharmonic frequency calculations suggest that changing the substitution position of the azide group from para to meta can effectively modulate the FRs by reducing the coupling strength. This work provides a deep understanding of the FRs in azido-modified aromatic amino acids and sheds light on the modification of azido-modified amino acids for wider utilization as vibrational probes.