5-Phenylvaleric acid
(Synonyms: 5-苯基戊酸,5-Phenylpentanoic acid) 目录号 : GC62814
5-Phenylvaleric acid (Benzenepentanoic acid, Phenylpentanoic acid, Phenylvaleric Acid) is a Pentanoic acid of bacterial origin, occasionally found in human biofluids.
Cas No.:2270-20-4
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
5-Phenylvaleric acid (Benzenepentanoic acid, Phenylpentanoic acid, Phenylvaleric Acid) is a Pentanoic acid of bacterial origin, occasionally found in human biofluids.
| Cas No. | 2270-20-4 | SDF | |
| 别名 | 5-苯基戊酸,5-Phenylpentanoic acid | ||
| 分子式 | C11H14O2 | 分子量 | 178.23 |
| 溶解度 | 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。 |
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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 | 5.6107 mL | 28.0536 mL | 56.1073 mL |
| 5 mM | 1.1221 mL | 5.6107 mL | 11.2215 mL |
| 10 mM | 0.5611 mL | 2.8054 mL | 5.6107 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。
Structure and polymer form of poly-3-hydroxyalkanoates produced by Pseudomonas oleovorans grown with mixture of sodium octanoate/undecylenic acid and sodium octanoate/5-Phenylvaleric acid
Int J Biol Macromol 2007 Jan 30;40(2):112-8.PMID:16919325DOI:10.1016/j.ijbiomac.2006.06.017.
PHAs (poly-3-hydroxyalkanoates) obtained by Pseudomonas oleovorans grown with mixed carbon sources were investigated. Mixed carbon sources were sodium octanoate/undecylenic acid and sodium octanoate/5-Phenylvaleric acid. Effect of carbon source in pre-culture on PHAs structure was investigated. Main fermentation was conducted with mixture of sodium octanoate/undecylenic acid, and PHA contained both saturated and unsaturated units. When more undecylenic acid was used in the medium, the ratio of unsaturated unit increased and the T(g) of the products also changed. The PHA grown with mixture of sodium octanoate and undecylenic acid was a random copolymer, which was determined by DSC analysis. Using mixed carbon sources of sodium octanoate and 5-Phenylvaleric acid, highest dry cell weight and PHA concentration were obtained when 0.02g or 0.04g of 5-Phenylvaleric acid were added in 50mL medium. Cultured with sodium octanoate and 5-Phenylvaleric acid, PHA containing HO (3-hydroxyoctanoate) unit and HPV (3-hydroxy-5-phenylvalerate) unit was produced. T(g) of the products fell between those of pure PHO and pure PHPV. By means of DSC analysis and fractionation method, the PHA obtained was regarded as a random copolymer.
Intracellular degradation of two structurally different polyhydroxyalkanoic acids accumulated in Pseudomonas putida and Pseudomonas citronellolis from mixtures of octanoic acid and 5-Phenylvaleric acid
Int J Biol Macromol 2001 Dec 10;29(4-5):243-50.PMID:11718820DOI:10.1016/s0141-8130(01)00172-6.
From a set of mixed carbon sources, 5-Phenylvaleric acid (PV) and octanoic acid (OA), polyhydroxyalkanoic acid (PHA) was separately accumulated in the two pseudomonads Pseudomonas putida BM01 and Pseudomonas citronellolis (ATCC 13674) to investigate any structural difference between the two PHA accumulated under a similar culture condition using one-step culture technique. The resulting polymers were isolated by chloroform solvent extraction and characterized by fractional precipitation and differential scanning calorimetry. The solvent fractionation analysis showed that the PHA synthesized by P. putida was separated into two fractions, 3-hydroxy-5-phenylvalerate (3HPV))-rich PHA fraction in the precipitate phase and 3-hydroxyoctanoate (3HO)-rich PHA fraction in the solution phase whereas the PHA produced by P. citronellolis exhibited a rather little compositional separation into the two phases. According to the thermal analysis, the P. putida PHA exhibited two glass transitions indicative of the PHA not being homogeneous whereas the P. citronellolis PHA exhibited only one glass transition. It was found that the structural heterogeneity of the P. putida PHA was caused by a significant difference in the assimilation rate between PV and OA. The structural heterogeneity present in the P. putida PHA was also confirmed by a first order degradation kinetics analysis of the PHA in the cells. The two different first-order degradation rate constants (k(1)), 0.087 and 0.015/h for 3HO- and 3HPV-unit, respectively, were observed in a polymer system over the first 20 h of degradation. In the later degradation period, the disappearance rate of 3HO-unit was calculated to be 0.020 h. The k(1) value of 0.083/h, almost the same as for the 3HO-unit in the P. putida PHA, was obtained for the P(3HO) accumulated in P. putida BM01 grown on OA as the only carbon source. In addition, the k(1) value of 0.015/h for the 3HPV-unit in the P. putida PHA, was also close to 0.019/h for the P(3HPV) homopolymer accumulated in P. putida BM01 grown on PV plus butyric acid. On the contrary, the k(1) values for the P. citronellolis PHA were determined to be 0.035 and 0.029/h for 3HO- and 3HPV-unit, respectively, thus these two relatively close values implying a random copolymer nature of the P. citronellolis PHA. In addition, the faster degradation of P(3HO) than P(3HPV) by the intracellular P. putida PHA depolymerase indicates that the enzyme is more specific against the aliphatic PHA than the aromatic PHA.
Predicting solute partitioning in lipid bilayers: Free energies and partition coefficients from molecular dynamics simulations and COSMOmic
J Chem Phys 2014 Jul 28;141(4):045102.PMID:25084963DOI:10.1063/1.4890877.
Quantitative predictions of biomembrane/water partition coefficients are important, as they are a key property in pharmaceutical applications and toxicological studies. Molecular dynamics (MD) simulations are used to calculate free energy profiles for different solutes in lipid bilayers. How to calculate partition coefficients from these profiles is discussed in detail and different definitions of partition coefficients are compared. Importantly, it is shown that the calculated coefficients are in quantitative agreement with experimental results. Furthermore, we compare free energy profiles from MD simulations to profiles obtained by the recent method COSMOmic, which is an extension of the conductor-like screening model for realistic solvation to micelles and biomembranes. The free energy profiles from these molecular methods are in good agreement. Additionally, solute orientations calculated with MD and COSMOmic are compared and again a good agreement is found. Four different solutes are investigated in detail: 4-ethylphenol, propanol, 5-Phenylvaleric acid, and dibenz[a,h]anthracene, whereby the latter belongs to the class of polycyclic aromatic hydrocarbons. The convergence of the free energy profiles from biased MD simulations is discussed and the results are shown to be comparable to equilibrium MD simulations. For 5-Phenylvaleric acid the influence of the carboxyl group dihedral angle on free energy profiles is analyzed with MD simulations.
Mechanism-based inactivation of cytochromes P450 2E1 and 2B1 by 5-phenyl-1-pentyne
Arch Biochem Biophys 1998 Jun 15;354(2):295-302.PMID:9637739DOI:10.1006/abbi.1998.0679.
A series of acetylenic compounds whose structures were based on "P450 2E1-like" substrates was investigated for their ability to cause inactivation of P450 2E1-dependent p-nitrophenol hydroxylation. The most effective compound with liver microsomes from pyridine-treated rats or with rabbit P450 2E1 in a reconstituted system was 5-phenyl-1-pentyne. The inactivation of purified 2B1, 2E1, a truncated 2E1 lacking amino acids 3-29, 2E1(Delta3-29), or a truncated 2E1 in which threonine 303 was replaced with alanine, 2E1(Delta3-29, T303A), in a reconstituted system by 5-phenyl-1-pentyne was NADPH- and time-dependent and followed pseudo-first-order kinetics. The maximal rate constants for inactivation, the concentrations that gave half-maximal inactivation (KI), and the partition ratios (the number of 5-Phenylvaleric acid molecules formed/inactivation event) were determined with each P450. The KI values for 2B1 and 2E1(Delta3-29, T303A) were twice those for 2E1 and 2E1(Delta3-29), and the partition ratios for 2B1 and 2E1(Delta3-29, T303A) were 5-10 times greater than those of 2E1 or 2E1(Delta3-29). During the incubation of P450 2E1 with 5-phenyl-1-pentyne, the loss of P450 as determined by the reduced-CO difference spectra was equal to the loss of catalytic activity. The formation of a heme adduct was demonstrated by HPLC analysis of reaction mixtures containing 5-[3H]phenyl-1-pentyne. HPLC analysis with diode-array detection showed that the Soret region of the proposed heme adduct was different from that of the unmodified heme. The HPLC peak containing the proposed heme adduct was further analyzed by matrix-assisted laser desorption ionization mass spectrometry, and the resulting peaks could result from the addition of a 2-oxo-5-phenylpentyl group to the heme.
Sequential production of two different polyesters in the inclusion bodies of Pseudomonas oleovorans
Int J Biol Macromol 1996 Jul;19(1):29-34.PMID:8782716DOI:10.1016/0141-8130(96)01096-3.
When Pseudomonas oleovorans was grown on a mixture of 5-Phenylvaleric acid, PVA, and nonanoic acid, NA, the reserve polyester produced included both a homopolymer and a copolymer. The homopolymer poly-3-hydroxy-5-phenylvalerate, PHPV, contained only 3-hydroxy-5-phenylvalerate units, while the copolymer contained the same long chain 3-hydroxyalkanoates as those present in the copolymer poly-3-hydroxynonanoate, PHN, which is produced from acid alone. The intracellular location of each of these polymers was determined by selective staining of the inclusion body granules with ruthenium tetraoxide and examination by transmission electron microscopy showed that both types of polyesters occurred in the same granule. PHN was present in the center of the granule, while PHPV accumulated around the PHN in the inclusion body. The proteins associated with the inclusion bodies were separated using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). In all cases, two different polymerase enzymes of molecular weight 59 and 55 KDa were present, indicating that the same polymerase enzyme system was responsible for the production of both PHN and PHPV. Attempts were made to produce a random copolymer containing both alkyl and phenylalkyl repeat units by varying the growth conditions, but a mixture of PHN and PHPV was always produced instead.