Prolylleucine
(Synonyms: ((Benzyloxy)carbonyl)-L-prolyl-D-leucine) 目录号 : GC32626
脯氨酰亮氨酸是一种含有支链氨基酸的二肽。
Cas No.:61596-47-2
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >99.50%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Prolylleucine is a dipeptide containing branched-chain amino acids.
The addition of specific dipeptide containing branched-chain amino acids, such as Prolylleucine, to the growth medium negatively affects cell envelope-associated proteinase (CEP) activity, whereas dipeptides without branched-chain amino acids had no effect on the enzyme's production. To determine if certain peptides are involved in the regulation of CEP biosynthesis, eight specific dipeptides, one tripeptide, and two peptide fractions (LMMP and HMMP) from Casitone are evaluated. The CEP activity levels of L. delbrueckii subsp. lactis CRL 581 grown in MDM supplemented with LMMP are similar to those obtained in cells grown in minimal defined medium (MDM) supplemented with Casitone (99-fold reduction). The addition of leucylglycylglycine (LGG), leucylleucine (LL), leucylproline (LP), or Prolylleucine (PL) (final concentration, 1 mM) to MDM leads to a 6.5-, 7-, 4-, or 3.5-fold reduction in CEP activity, respectively. An increase of up to 5 mM in the concentration of these dipeptides results in a further two- or threefold reduction of CEP activity compared to the activity obtained in the presence of 1 mM of the peptide mentioned above. LGG, LL, LP, and Prolylleucine contain leucine as a branched-chain amino acid (BCAA). In contrast, no effect on CEP activity is observed by the supplementation of MDM with 1 to 5 mM of GT, PA, TG, GM, GP (dipeptides without BCAA), or HMMP. No inhibitory effect on proteinase activity from the presence of high concentrations (10-fold increase) of each of the 20 amino acids in the growth medium is observed. However, a 50-fold increase in BCAA concentration in MDM leads to a repression of proteinase synthesis of 40%. L. delbrueckii subsp. lactis is auxotrophic for BCAA[1].
[1]. Hebert EM, et al. Characterization of the pattern of alphas1- and beta-casein breakdown and release of a bioactive peptide by a cell envelope proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581. Appl Environ Microbiol. 2008 Jun;74(12):3682-9.
| Cas No. | 61596-47-2 | SDF | |
| 别名 | ((Benzyloxy)carbonyl)-L-prolyl-D-leucine | ||
| Canonical SMILES | Z-Pro-{d-Leu} | ||
| 分子式 | C19H26N2O5 | 分子量 | 362.42 |
| 溶解度 | DMSO : ≥ 100 mg/mL (275.92 mM) | 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 | 2.7592 mL | 13.7961 mL | 27.5923 mL |
| 5 mM | 0.5518 mL | 2.7592 mL | 5.5185 mL |
| 10 mM | 0.2759 mL | 1.3796 mL | 2.7592 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。
Unraveling the Serum Metabolomic Profile of Acrylamide-Induced Cardiovascular Toxicity
J Agric Food Chem 2021 Oct 13;69(40):12012-12020.PMID:34586797DOI:10.1021/acs.jafc.1c04367.
Acrylamide has been reported as an important dietary risk factor from carbohydrate-rich processing food. However, systemic biological effects on the serum metabolomics induced by acrylamide have poorly been understood. In the present study, we evaluated the metabolic profiles in a rat serum after exposure to acrylamide using ultrahigh-performance liquid chromatography combined with quadrupole-orbitrap high-resolution mass spectrometry. The serum biochemical parameters of the treated and control groups were also determined using an automatic biochemical analyzer. Compared with the control group, 10 metabolites were significantly upregulated, including citric acid, d-(-)-fructose, gluconic acid, l-ascorbic acid 2-sulfate, 2-hydroxycinnamic acid, valine, l-phenylalanine, Prolylleucine, succinic acid, and cholic acid, while 5 metabolites were significantly downregulated, including 3-hydroxybutyric acid, 4-oxoproline, 2,6-xylidine, 4-phenyl-3-buten-2-one, and N-ethyl-N-methylcathinone in the serum of 4-week-old rats exposed to acrylamide in the high-dose group (all P < 0.05). Importantly, acrylamide exposure affected metabolites mainly involved in the citrate cycle, valine, leucine, and isoleucine biosyntheses, phenylalanine, tyrosine and tryptophan biosyntheses, and pyruvate metabolism. These results suggested that exposure to acrylamide in rats exhibited marked systemic metabolic changes and affected the cardiovascular system. This study will provide a theoretical basis for exploring the toxic mechanism and will contribute to the diagnosis and prevention of acrylamide-induced cardiovascular toxicity.
Regulation of Proteolytic Enzyme Activity in Lactococcus lactis
Appl Environ Microbiol 1996 Jan;62(1):156-61.PMID:16535207DOI:10.1128/aem.62.1.156-161.1996.
Two different Lactococcus lactis host strains, L. lactis subsp. lactis MG1363 and L. lactis subsp. cremoris SK1128, both containing plasmid pNZ521, which encodes the extracellular serine proteinase (PrtP) from strain SK110, were used to study the medium and growth-rate-dependent activity of three different enzymes involved in the proteolytic system of lactococci. The activity levels of PrtP and both the intracellular aminopeptidase PepN and the X-prolyl-dipeptidyl aminopeptidase PepXP were studied during batch and continuous cultivation. In both strains, the PrtP activity level was regulated by the peptide content of the medium. The highest activity level was found during growth in milk, and the lowest level was found during growth in the peptide-rich laboratory medium M17. Regulation of the intracellular peptidase activity appeared to be a strain-dependent phenomenon. In cells of strain MG1363, the activity levels of PepN and PepXP were regulated in a similar way to that observed for PrtP. In cells of strain SK1128, the levels of both peptidases were not significantly influenced by the peptide content of the medium. The presence of specific concentrations of the dipeptide Prolylleucine could mimic the low activity levels of the regulated proteolytic enzymes, even to the activity level found on M17 medium. The effect of the presence of the dipeptide Prolylleucine in the medium on the activity level of the regulated proteolytic enzymes was confirmed at fixed growth rates in chemostat cultures.
Detection of Pork in Beef Meatballs Using LC-HRMS Based Untargeted Metabolomics and Chemometrics for Halal Authentication
Molecules 2022 Nov 29;27(23):8325.PMID:36500423DOI:10.3390/molecules27238325.
Adulteration of high-quality meat products using lower-priced meats, such as pork, is a crucial issue that could harm consumers. The consumption of pork is strictly forbidden in certain religions, such as Islam and Judaism. Therefore, the objective of this research was to develop untargeted metabolomics using liquid chromatography-high resolution mass spectrometry (LC-HRMS) combined with chemometrics for analysis of pork in beef meatballs for halal authentication. We investigated the use of non-targeted LC-HRMS as a method to detect such food adulteration. As a proof of concept using six technical replicates of pooled samples from beef and pork meat, we could show that metabolomics using LC-HRMS could be used for high-throughput screening of metabolites in meatballs made from beef and pork. Chemometrics of principal component analysis (PCA) was successfully used to differentiate beef meatballs and pork meatball samples. Partial least square-discriminant analysis (PLS-DA) clearly discriminated between halal and non-halal beef meatball samples with 100% accuracy. Orthogonal projection to latent structures-discriminant analysis (OPLS-DA) perfectly discriminated and classified meatballs made from beef, pork, and a mixture of beef-pork with a good level of fitness (R2X = 0.88, R2Y = 0.71) and good predictivity (Q2 = 0.55). Partial least square (PLS) and orthogonal PLS (OPLS) were successfully applied to predict the concentration of pork present in beef meatballs with high accuracy (R2 = 0.99) and high precision. Thirty-five potential metabolite markers were identified through VIP (variable important for projections) analysis. Metabolites of 1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine, acetyl-l-carnitine, dl-carnitine, anserine, hypoxanthine, linoleic acid, and Prolylleucine had important roles for predicting pork in beef meatballs through S-line plot analysis. It can be concluded that a combination of untargeted metabolomics using LC-HRMS and chemometrics is promising to be developed as a standard analytical method for halal authentication of highly processed meat products.
[Influence of changes in the state of brain neurotransmitter and peptidergic systems on circadian rhythms and behavior of rats]
Zh Vyssh Nerv Deiat Im I P Pavlova 2012 Jul-Aug;62(4):453-64.PMID:23035562doi
The influence of changes in the state of a number of neurotransmitter and peptidergic brain systems on the circadian rhythms and behaviour of rats was studied. Prolylleucine (oxytocine dipeptide fragment) eliminates disorders of circadian motility rhythm in SHR rats induced by "injection" stress, impedes dysrhythmias caused by application of cholinergic and glutamatergic modulators in SHR and WKY rats, and prevents cognitive disorders in SHR rats produced by REM sleep deprivation.
Transcriptional pattern of genes coding for the proteolytic system of Lactococcus lactis and evidence for coordinated regulation of key enzymes by peptide supply
J Bacteriol 2001 Jun;183(12):3614-22.PMID:11371525DOI:10.1128/JB.183.12.3614-3622.2001.
The transcription of 16 genes encoding 12 peptidases (pepC, pepN, pepX, pepP, pepA, pepF2, pepDA1, pepDA2, pepQ, pepT, pepM, and pepO1), P(I) and P(III) proteinases (prtP1 and prtP3), and three transport systems (dtpT, dtpP, and opp-pepO1) of Lactococcus lactis MG1363 was analyzed in response to different environmental factors. Promoter fusions with luciferase reporter genes and/or mRNA analysis were used to study the effects of sugar sources, growth at 37 degrees C, and peptide supply on the transcription of these genes. Only transcription of the pepP gene is modulated by the source of sugar. The presence of potential catabolite-responsive element (CRE) boxes in its promoter region suggests that expression of this gene is directly controlled by catabolic repression. Elevated temperature had no significant effect on the level of transcription of these genes. prtP1, prtP3, pepC, pepN, pepX, and the opp-pepO1 operon are the most highly expressed genes in chemically defined medium, and their expression is repressed 5- to 150-fold by addition of peptide sources such as Casitone in the medium. Moreover, the transcription of prtP1, prtP3, pepC, pepN, and the opp-pepO1 operon is repressed two- to eight-fold by the dipeptides leucylproline and Prolylleucine. The transcription of pepDA2 might also be repressed by the peptide sources, but this effect is not observed on the regulation of dtpT, pepP, pepA, pepF2, pepDA1, pepQ, pepT, pepM, and the dtpP operon. The significance of these results with respect to the functions of different components of the proteolytic system in L. lactis are discussed.