12-Hydroxydodecanoic Acid

12-hydroxylauric acid is a medium-chain fatty acid that is the 12-hydroxylated derivative of lauric acid. It has a role as a human metabolite. It is an omega-hydroxy fatty acid and a medium-chain fatty acid. It derives from a dodecanoic acid. It is a conjugate acid of a 12-hydroxylaurate.

Expression of CYP4V2 in human THP1 macrophages and its transcriptional regulation by peroxisome proliferator-activated receptor gamma.[Pubmed:28729181]

Toxicol Appl Pharmacol. 2017 Sep 1;330:100-106.

Because macrophages respond to a variety of pathological and pharmacological reagents, understanding the role of P450s in macrophages is important for therapeutic intervention. There has been a lack of research on CYP4 in macrophages, but fatty acid accumulation and lipid trafficking in macrophages have been suggested to be a main cause of atherosclerosis. All human CYP4 genes (n=12) were screened in THP1 macrophages by gene-specific reverse transcriptase-polymerase chain reaction (RT-PCR). Only CYP4V2 exhibited strong expression of both mRNA and protein. Expression levels of both CYP4V2 mRNA and protein were significantly reduced after treatment with peroxisome proliferator-activated receptor gamma (PPARgamma) antagonist GW9662. However, the expression levels of CYP4V2 were not changed by PPARalpha antagonist (GW6471) and liver X receptor alpha antagonist (22-S hydroxycholesterol). A metabolite of the CYP4V2 enzyme, 12-Hydroxydodecanoic Acid, was detected in THP1 macrophages, and this metabolite was significantly decreased after treatment with the PPARgamma inhibitor GW9662 (>80% decreased, p<0.05). In summary, fatty acid metabolizing protein CYP4V2 was identified in human THP1 macrophages, and its expression was regulated by PPARgamma. Further study is required to understand the role of CYP4V2 with regard to fat accumulation in the activated macrophage and atherosclerotic plaque development.

Structural profiling of wax biopolymer from Pinus roxburghii Sarg. needles using spectroscopic methods.[Pubmed:28596007]

Int J Biol Macromol. 2017 Nov;104(Pt A):261-273.

Pinus roxburghii Sarg. is the most abundant species in Himalayan region. The needles of the species largely contribute to the forest biomass and remain the major cause of forest fires leading to climate change, biodiversity loss, etc. Intriguingly, the layer of needles contains wax, a biomacromolecule with potential chemical functionalities for value addition. In the present study, a distinctive approach towards complete structural analysis of the isolated wax in its native state has been done using (1)H, (13)C, HSQC, HMBC, COSY, TOCSY along with GC-MS of the methyl esters of constituent fatty acids. The wax was isolated in a quantitative yield of 1.64% and analyses suggest that it is a polymer of linearly attached fatty acid esters which on hydrolysis yielded three types of omega-hydroxy fatty acids viz. 12-Hydroxydodecanoic Acid, 14-hydroxytetradecanoic acid and 16-hydroxyhexadecanoic acid in a ratio of 1:1:2 respectively. Complete assignments for a carbonyl group, alpha-, beta- and other methylenes present in wax were achieved; corroborating the presence of polyester. In particular, identification of wax structure was accomplished through NMR; thereby providing a lead towards future structural analysis of waxes in their native form. The study would also be helpful to generate commercially important compounds derived from pine needle wax. This will offer an opportunity for utilisation of pine needle biomass: a root cause of Himalayan forest fires.

A Comprehensive Analysis of Metabolomics and Transcriptomics in Cervical Cancer.[Pubmed:28225065]

Sci Rep. 2017 Feb 22;7:43353.

Cervical cancer (CC) still remains a common and deadly malignancy among females in developing countries. More accurate and reliable diagnostic methods/biomarkers should be discovered. In this study, we performed a comprehensive analysis of metabolomics (285 samples) and transcriptomics (52 samples) on the potential diagnostic implication and metabolic characteristic description in cervical cancer. Sixty-two metabolites were different between CC and normal controls (NOR), in which 5 metabolites (bilirubin, LysoPC(17:0), n-oleoyl threonine, 12-Hydroxydodecanoic Acid and tetracosahexaenoic acid) were selected as candidate biomarkers for CC. The AUC value, sensitivity (SE), and specificity (SP) of these 5 biomarkers were 0.99, 0.98 and 0.99, respectively. We further analysed the genes in 7 significantly enriched pathways, of which 117 genes, that were expressed differentially, were mainly involved in catalytic activity. Finally, a fully connected network of metabolites and genes in these pathways was built, which can increase the credibility of our selected metabolites. In conclusion, our biomarkers from metabolomics could set a path for CC diagnosis and screening. Our results also showed that variables of both transcriptomics and metabolomics were associated with CC.

Chemical constituents of Antrodia camphorata submerged whole broth.[Pubmed:18855215]

Nat Prod Res. 2008;22(13):1151-7.

One new compound, 10-hydroxy-gamma-dodecalactone (1) and three natural new compounds, 11-hydroxy-gamma-dodecalactone (2), 2-(2-hydroxyethyl)phenol (3) and 12-Hydroxydodecanoic Acid methyl ester (4), together with eight known compounds, ergostatrien-3beta-ol, ergosterol peroxide, methyl (4-hydroxyphenyl)acetate, vanillin, 4-hydroxybenzaldehyde, hexadecanoic acid, 5-methoxymethylfuran-2-carbaldehyde and 5-hydroxymethylfuran-2-carbaldehyde, all were isolated from the submerged whole broth of Antrodia camphorata. The structures of 1 and 2 were principally elucidated by spectral evidence and the absolute configuration was elucidated by the modified Mosher's method.

Lipase-catalyzed synthesis and properties of poly[(12-hydroxydodecanoate)-co-(12-hydroxystearate)] directed towards novel green and sustainable elastomers.[Pubmed:17955511]

Macromol Biosci. 2008 Jan 9;8(1):38-45.

Novel green and sustainable elastomers having both good biodegradability and chemical recyclability properties were designed and synthesized using potentially biobased materials and lipase as an environmentally benign catalyst. High molecular weight poly[(12-hydroxydodecanoate)-co-(12-hydroxystearate)] [poly(12HD-co-12HS)] samples with varying monomer ratios were prepared by the polycondensation of 12-Hydroxydodecanoic Acid and methyl 12-hydroxystearate using immobilized lipase from Candida antarctica (IM-CA) in toluene in the presence of molecular sieves 4A at 90 degrees C. Although poly(12HD) is a highly crystalline polyester having a melting temperature (T(m)) of 87.6 degrees C and crystalline temperature (T(c)) of 64 degrees C, by the copolymerization of 12HD with 12HS, both the T(m) and T(c) of the copolymer decreased with increasing 12HS contents, and poly(12HD-co-12HS) containing more than 60 mol-% 12HS was a viscous liquid at room temperature. At the same time, the Young's modulus and hardness also decreased with increasing 12HS content, and poly(12HD-co-36 mol-% 12HS) exhibited an elastic behavior, having a hardness of 70 A using a durometer A. In addition, it showed an excellent biodegradability by activated sludge and chemical recyclability by lipase.

Encapsulation and exfoliation of inorganic lamellar fillers into polycaprolactone by electrospinning.[Pubmed:17824642]

Biomacromolecules. 2007 Oct;8(10):3147-52.

The present paper reports, for the first time, the successful fabrication of layered double hydroxide (Mg-Al LDH)-reinforced polycaprolactone (PCL) nanofibers by electrospinning. Either the LDH in carbonate form or an LDH organically modified with 12-Hydroxydodecanoic Acid (LDH-HA) were incorporated into PCL and electrospun using a voltage of 20 KV. The LDH-HA was prepared by an ionic exchange reaction from pristine LDH and encapsulated into PCL from acetone solutions at 15 wt %. The morphological analysis showed pure PCL fibers with an average diameter of 600 +/- 50 nm, and this dimension was maintained in the fibers with LDH, with the inorganic component residing outside the fibers and not exfoliated. At variance, the fibers with the LDH-HA showed a significantly lower average diameter in the range of 350 +/- 50 nm, indicating the improved electrospinnability of PCL. Moreover, the inorganic lamellae were exfoliated, as shown by X-rays and residing inside the nanofibers as demonstrated by energy dispersive X-ray spectroscopy analysis. The structural parameters, such as degradation temperature and crystallinity, were investigated for all the samples and correlated with the electrospinning process.

Functional expression and characterization of cytochrome P450 52A21 from Candida albicans.[Pubmed:17400174]

Arch Biochem Biophys. 2007 Aug 15;464(2):213-20.

Candida albicans contains 10 putative cytochrome P450 (CYP) genes coding for enzymes that appear to play important roles in fungal survival and virulence. Here, we report the characterization of CYP52A21, a putative alkane/fatty acid hydroxylase. The recombinant CYP52A21 protein containing a 6x(His)-tag was expressed in Escherichia coli and was purified. The purified protein, reconstituted with rat NADPH-cytochrome P450 reductase, omega-hydroxylated dodecanoic acid to give 12-Hydroxydodecanoic Acid, but to a lesser extent also catalyzed (omega-1)-hydroxylation to give 11-hydroxydodecanoic acid. When 12,12,12-d(3)-dodecanoic acid was used as the substrate, there was a major shift in the oxidation from the omega- to the (omega-1)-hydroxylated product. The regioselectivity of fatty acid hydroxylation was examined with the 12-iodo-, 12-bromo-, and 12-chlorododecanoic acids. Although all three 12-halododecanoic acids bound to CYP52A21 with similar affinities, the production of 12-oxododecanoic acid decreased as the size of the terminal halide increased. The regioselectivity of CYP52A21 fatty acid oxidation is thus consistent with presentation of the terminal end of the fatty acid chain for oxidation via a narrow channel that limits access to other atoms of the fatty acid chain. This constricted access, in contrast to that proposed for the CYP4A family of enzymes, does not involve covalent binding of the heme to the protein.

Structure-function relationships in human glutathione-dependent formaldehyde dehydrogenase. Role of Glu-67 and Arg-368 in the catalytic mechanism.[Pubmed:16605250]

Biochemistry. 2006 Apr 18;45(15):4819-30.

The active-site zinc in human glutathione-dependent formaldehyde dehydrogenase (FDH) undergoes coenzyme-induced displacement and transient coordination to a highly conserved glutamate residue (Glu-67) during the catalytic cycle. The role of this transient coordination of the active-site zinc to Glu-67 in the FDH catalytic cycle and the associated coenzyme interactions were investigated by studying enzymes in which Glu-67 and Arg-368 were substituted with Leu. Structures of FDH.adenosine 5'-diphosphate ribose (ADP-ribose) and E67L.NAD(H) binary complexes were determined. Steady-state kinetics, isotope effects, and presteady-state analysis of the E67L enzyme show that Glu-67 is critical for capturing the substrates for catalysis. The catalytic efficiency (V/K(m)) of the E67L enzyme in reactions involving S-nitrosoglutathione (GSNO), S-hydroxymethylglutathione (HMGSH) and 12-Hydroxydodecanoic Acid (12-HDDA) were 25 000-, 3000-, and 180-fold lower, respectively, than for the wild-type enzyme. The large decrease in the efficiency of capturing GSNO and HMGSH by the E67L enzyme results mainly because of the impaired binding of these substrates to the mutant enzyme. In the case of 12-HDDA, a decrease in the rate of hydride transfer is the major factor responsible for the reduction in the efficiency of its capture for catalysis by the E67L enzyme. Binding of the coenzyme is not affected by the Glu-67 substitution. A partial displacement of the active-site zinc in the FDH.ADP-ribose binary complex indicates that the disruption of the interaction between Glu-67 and Arg-368 is involved in the displacement of active-site zinc. Kinetic studies with the R368L enzyme show that the predominant role of Arg-368 is in the binding of the coenzyme. An isomerization of the ternary complex before hydride transfer is detected in the kinetic pathway of HMGSH. Steps involved in the binding of the coenzyme to the FDH active site are also discerned from the unique conformation of the coenzyme in one of the subunits of the E67L.NAD(H) binary complex.

A structural study of amphiphilic PAMAM (poly(amido amine)) dendrimers in Langmuir and Langmuir-Blodgett films.[Pubmed:16290673]

J Colloid Interface Sci. 2002 Jun 15;250(2):364-70.

Two amphiphilic PAMAM dendrimers are synthesized by attaching 12-Hydroxydodecanoic Acid (HA) chains to a poly(amido amine) (PAMAM) dendrimer core (including generation I and generation II). The limiting molecular area obtained from the surface pressure-area isotherm at the air/water interface suggests the edge-on configuration for both dendrimers in Langmuir films. The edge-on arrangement is also supported by the atomic force microscopic (AFM) studies of the Langmuir-Blodgett films.

Calibration of the channel that determines the omega-hydroxylation regiospecificity of cytochrome P4504A1: catalytic oxidation of 12-HALODOdecanoic acids.[Pubmed:15849199]

J Biol Chem. 2005 Jun 17;280(24):22697-705.

The fatty acid omega-hydroxylation regiospecificity of CYP4 enzymes may result from presentation of the terminal carbon to the oxidizing species via a narrow channel that restricts access to the other carbon atoms. To test this hypothesis, the oxidation of 12-iodo-, 12-bromo-, and 12-chlorododecanoic acids by recombinant CYP4A1 has been examined. Although all three 12-halododecanoic acids bind to CYP4A1 with similar dissociation constants, the 12-chloro and 12-bromo fatty acids are oxidized to 12-Hydroxydodecanoic Acid and 12-oxododecanoic acid, whereas the 12-iodo analogue is very poorly oxidized. Incubations in H(2)(18)(2)O show that the 12-Hydroxydodecanoic Acid oxygen derives from water, whereas that in the aldehyde derives from O(2). The alcohol thus arises from oxidation of the halide to an oxohalonium species that is hydrolyzed by water, whereas the aldehyde arises by a conventional carbon hydroxylation-elimination mechanism. No irreversible inactivation of CYP4A1 is observed during 12-halododecanoic acid oxidation. Control experiments show that CYP2E1, which has an omega-1 regiospecificity, primarily oxidizes 12-halododecanoic acids to the omega-aldehyde rather than alcohol product. Incubation of CYP4A1 with 12,12-[(2)H](2)-12-chlorododecanoic acid causes a 2-3-fold increase in halogen versus carbon oxidation. The fact that the order of substrate oxidation (Br > Cl >> I) approximates the inverse of the intrinsic oxidizability of the halogen atoms is consistent with presentation of the halide terminus via a channel that accommodates the chloride and bromide but not iodide atoms, which implies an effective channel diameter greater than 3.90 Angstroms but smaller than 4.30 Angstroms.

Mild, solvent-free omega-hydroxy acid polycondensations catalyzed by candida antarctica lipase B.[Pubmed:14715009]

Biomacromolecules. 2004 Jan-Feb;5(1):62-8.

Immobilized Candida antarctica Lipase B (Novozyme-435) was studied for bulk polyesterifications of linear aliphatic hydroxyacids of variable chain length. The products formed were not fractionated by precipitation. The relative reactivity of the hydroxyacids was l6-hydroxyhexadecanoic acid approximately 12-Hydroxydodecanoic Acid approximately 10-hydroxydecanoic acid (DPavg congruent with 120, Mw/Mn 6-hydroxyhexanoic acid (DPavg congruent with 80, Mw/Mn < or = 1.5, 48 h, 90 degrees C). Remarkable improvements in molecular-weight buildup resulted from leaving water in the reaction. By 4 h, without application of vacuum, the DPavg for 12- and 16-carbon hydroxyacids was about 90. In contrast, with identical substrates and water removal, the DPavg at 4 h was about 23. Large differences in the molecular-weight build up of 12-Hydroxydodecanoic Acid were observed for catalyst concentrations (%-by-wt relative to monomer) of 0.1, 0.5, 1, and 10. Nevertheless, by 24 h, with 1% catalyst containing 0.1% lipase, poly(12-Hydroxydodecanoic Acid) with Mn 17 600 was formed. For 12-Hydroxydodecanoic Acid polymerization at 90 degrees C, the catalyst activity decreased by 7, 18, and 25% at reaction times of 4, 24, and 48 h, respectively. Furthermore, the retention of catalyst activity was invariable as a function of the substrates used.

12-Hydroxydodecanoic acid is an endogenous metabolite.

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