Biliverdin (hydrochloride)
目录号 : GC42932An antioxidant bile pigment
Cas No.:856699-18-8
Sample solution is provided at 25 µL, 10mM.
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- Purity: >95.00%
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- Datasheet
Biliverdin is a green bile pigment produced from the oxidation of heme in a reaction catalyzed by heme oxygenase and is further reduced to bilirubin by biliverdin reductase.[1][2] Biliverdin regulates the cellular heme degradation process by inhibiting substrates from binding to the catalytic site of heme oxygenase. Bile pigments such as biliverdin are known to possess anti-mutagenic and antioxidant properties.[3][4]
Reference:
[1]. Liu, Y., Moënne-Loccoz, P., Loehr, T.M., et al. Heme oxygenase-1, intermediates in verdoheme formation and the requirement for reduction equivalents. The Journal of Biological Chemisty 272, 6909-6917 (1997).
[2]. Maines, M.D. The heme oxygenase system: A regulator of second messenger gases. Annu. Rev. Pharmacol. Toxicol. 37, 517-554 (1997).
[3]. Bulmer, A.C., Ried, K., Blanchfield, J.T., et al. The anti-mutagenic properties of bile pigments. Mutation Research 658(1-2), 28-41 (2008).
[4]. Mölzer, C., Huber, H., Steyrer, A., et al. In vitro antioxidant capacity and antigenotoxic properties of protoporphyrin and structurally related tetrapyrroles. Free Rad.Res. 46(11), 1369-1377 (2012).
| Cas No. | 856699-18-8 | SDF | |
| 化学名 | 3,18-diethenyl-1,19,22,24-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-21H-biline-8,12-dipropanoic acid, monohydrochloride | ||
| Canonical SMILES | OC(CCC1=C(/C=C2C(CCC(O)=O)=C(C)C(/C=C3NC(C(C=C)=C\3C)=O)=N/2)NC(/C=C4NC(C(C)=C\4C=C)=O)=C1C)=O.Cl | ||
| 分子式 | C33H34N4O6•HCl | 分子量 | 619.1 |
| 溶解度 | 20mg/mL in DMSO, 20mg/mL in DMF | 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 | 1.6152 mL | 8.0762 mL | 16.1525 mL |
| 5 mM | 0.323 mL | 1.6152 mL | 3.2305 mL |
| 10 mM | 0.1615 mL | 0.8076 mL | 1.6152 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。
The biliverdin-bilirubin antioxidant cycle of cellular protection: Missing a wheel?
Free Radic Biol Med 2010 Sep 1;49(5):814-20.PMID:20547221DOI:10.1016/j.freeradbiomed.2010.06.001.
Bilirubin reportedly protects cultured cells from the toxicity of a 10,000-fold molar excess of H(2)O(2). A bilirubin-biliverdin cycling mechanism has been proposed to explain this remarkable effect whereby bilirubin reacts with oxyradicals specifically generating Biliverdin, which is then reduced back to bilirubin by NADPH/Biliverdin reductase. Chemical evidence for this mechanism was formation of Biliverdin during incubation of bilirubin-albumin with 2,2'-azobis(2-amidinopropane) hydrochloride (AAPH) in vitro and the assumption that Biliverdin was formed by the reaction of peroxyl radicals with bilirubin. This paper describes spectroscopic studies on the reaction of bilirubin with AAPH in the presence and absence of human serum albumin. Reactions were run in air and also under oxygen-depleted and oxygen-saturated solutions, the former to inhibit peroxyl radical formation, the latter to augment it. The results confirm that degradation of bilirubin, rather than dehydrogenation to Biliverdin, predominates in the reaction of bilirubin with peroxyl radicals generated by AAPH thermolysis. They also suggest that Biliverdin produced in the presence of albumin is not formed by the reaction of bilirubin with alkyl peroxyl radicals, as previously assumed. The observations undermine the plausibility of the bilirubin-biliverdin recycling mechanism proposed to explain the reported hyperprotective effect of bilirubin on mammalian cells exposed to excess H(2)O(2).
Activation of human biliverdin-IXα reductase by urea: generation of kinetically distinct forms during the unfolding pathway
Biochim Biophys Acta 2013 Dec;1834(12):2573-8.PMID:24060811DOI:10.1016/j.bbapap.2013.09.009.
Activation of enzymes by low concentrations of denaturants has been reported for a limited number of enzymes including lipocalin-type prostaglandin D synthase (L-PGDS) and adenylate kinase. During unfolding studies on human biliverdin-IXα reductase it was discovered that the enzyme is activated at low concentrations of urea. Under standard assay conditions the native enzyme displays pronounced substrate inhibition with Biliverdin as variable substrate; however in the presence of 3M urea, the substrate inhibition is abolished and the enzyme exhibits Michaelian kinetics. When the initial rate kinetics with NADPH as variable substrate are conducted in 3M urea, the Vmax is increased 11-fold to 1.8μmol/min/mg and the apparent Km for Biliverdin increases from 1 to 3μM. We report the existence of two kinetically distinct folded intermediates between the native and unfolded forms. When the period of incubation with urea was varied prior to measuring enzyme activity, the apparent Vmax was shown to decay to half that seen at zero time with a half life of 5.8minutes, while the apparent Km for NADPH remains constant at approximately 5μM. With NADH as cofactor the half life of the activated (A) form was 2.9minutes, and this form decays in 3M urea to a less active (LA) form. The apparent Km for NADH increases from 0.33mM to 2mM for the A and LA forms. These kinetically distinct species are reminiscent of the activity-enhanced and inactive forms of L-PGDS observed in the presence of urea and guanidine hydrochloride.
Heme oxygenase 1-generated carbon monoxide and Biliverdin attenuate the course of experimental necrotizing pancreatitis
Pancreas 2013 Mar;42(2):265-71.PMID:23000891DOI:10.1097/MPA.0b013e318264cc8b.
Objective: The cytoprotective enzyme heme oxygenase 1 (HO-1) is highly up-regulated in acute pancreatitis (AP). In this study, we tested its metabolites as potential therapeutic agents for AP in rats. Methods: Acute necrotizing pancreatitis was induced by retrograde intraductal injection of sodium taurocholate in rats. Biliverdin hydrochloride (BV HCl) (50 μmol/kg subcutaneously), the carbon monoxide, donor methylene chloride (MC) (500 mg/kg orally), or iron-chelating desferrioxamine (DFO) (125 mg/kg subcutaneously) were administered in a therapeutic manner starting with the first dose 4 hours after taurocholate injection to mimic the effects of HO-1 metabolites. Results: Administration of BV HCl, MC, or DFO showed significant reduction of inflammatory activity in comparison to controls leading to lower myeloperoxidase activity in the pancreas, less edema, lower ascites volumes, and preservation of tissue integrity (P < 0.05). Administration of either BV HCl or MC markedly increased 5-day survival rate (70% and 75% vs 40%; P < 0.05), whereas DFO had no significant effect on survival (60%). When given in therapeutic manner, all 3 substances led to diminished nuclear factor κB activity in the pancreas (P < 0.05). Conclusions: Therapeutic use of BV HCl and MC led to marked reduction of mortality in experimental pancreatitis. Thus, HO-1 metabolites may present a novel therapeutic approach in AP treatment.
Stabilization of Near-Infrared Fluorescent Proteins by Packaging in Virus-like Particles
Biomacromolecules 2020 Jun 8;21(6):2432-2439.PMID:32441521DOI:10.1021/acs.biomac.0c00362.
Near-IR fluorescent Qβ virus-like particles (VLPs) were produced in a high yield by packaging highly red-shifted monomeric and dimeric versions of biliverdin-dependent fluorescent proteins within the capsid shell. The simple addition of Biliverdin hydrochloride to the medium during or after Escherichia coli protein expression was enough to produce fully matured encapsidated fluorophores. The packaged near-IR proteins exhibited identical photochemical properties to their nonencapsidated analogues but were far more stable toward heat, chaotrope-induced denaturation, and proteolysis. Noninvasive in vivo imaging showed the VLPs to traffic primarily to the liver after systemic injection in mice, revealing that the particles were easily detected by a standard instrument.
The Pathways of the iRFP713 Unfolding Induced by Different Denaturants
Int J Mol Sci 2018 Sep 15;19(9):2776.PMID:30223568DOI:10.3390/ijms19092776.
Near-infrared fluorescent proteins (NIR FPs) based on the complexes of bacterial phytochromes with their natural Biliverdin chromophore are widely used as genetically encoded optical probes for visualization of cellular processes and deep-tissue imaging of cells and organs in living animals. In this work, we show that the steady-state and kinetic dependencies of the various spectral characteristics of iRFP713, developed from the bacterial phytochrome RpBphP2 and recorded at protein unfolding induced by guanidine hydrochloride (GdnHCl), guanidine thiocyanate (GTC), and urea, differ substantially. A study of the unfolding of three single-tryptophan mutant forms of iRFP713 expectedly revealed that protein unfolding begins with the dissociation of the native dimer, while the monomers remain compact. A further increase in the denaturant concentration leads to the formation of an intermediate state of iRFP713 having hydrophobic areas exposed on the protein surface (I). The total surface charge of iRFP713 (pI 5.86) changes from negative to positive with an increase in the concentration of GdnHCl and GTC because the negative charge of glutamic and aspartic acids is neutralized by forming salt bridges between the carboxyl groups and GdnH⁺ ions and because the guanidinium cations bind to amide groups of glutamines and asparagines. The coincidence of both the concentration of the denaturants at which the intermediate state of iRFP713 accumulates and the concentration of GdnH⁺ ions at which the neutralization of the surface charge of the protein in this state is ensured results in strong protein aggregation. This is evidently realized by iRFP713 unfolding by GTC. At the unfolding of the protein by GdnHCl, an intermediate state is populated at higher denaturant concentrations and a strong aggregation is not observed. As expected, protein aggregates are not formed in the presence of the urea. The aggregation of the protein upon neutralization of the charge on the macromolecule surface is the main indicator of the intermediate state of protein. The unfolded state of iRFP713, whose formation is accompanied by a significant decrease in the parameter A, was found to have a different residual structure in the denaturants used.