PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Azides”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 613 records · Page 34Linked to original sources
PubMed2000

Synthesis of alpha-amino-alpha'-diazomethyl ketones via ring opening of substituted cyclopropanones with alkyl azides. A facile route to N-substituted 3-azetidinones.

[reaction: see text] The reaction of alkyl azides with triethyl(1-methoxy-2, 2-dimethyl-cyclopropoxy)silane affords a series of alpha-amino-alpha'-diazomethyl ketones in moderate yields (38-54%). The mechanism of this novel process is discussed. The diazomethyl ketones could also be cyclized to the corresponding N-substituted 3-azetidinones in good yield upon treatment with Rh(2)(OAc)(4).

Amines↗
PubMed2000

Staudinger ligation: a peptide from a thioester and azide.

[reaction: see text] The technique of native chemical ligation enables the total chemical synthesis of proteins. This method is limited, however, by an absolute requirement for a cysteine residue at the ligation juncture. Here, this restriction is overcome with a new chemical ligation method in which a phosphinobenzenethiol is used to link a thioester and azide. The product is an amide with no residual atoms.

Azides↗
PubMed2005

Highly efficient coupling of beta-substituted aminoethane sulfonyl azides with thio acids, toward a new chemical ligation reaction.

[reaction: see text] A highly efficient coupling of protected beta-substituted aminoethane sulfonyl azides with thio acids is reported. In the case of peptide thio acids, this method encompasses a new chemoselective ligation method. Furthermore, the resulting alpha-amino acyl sulfonamides can be alkylated with suitable electrophiles to obtain densely functionalized sulfonamide scaffolds.

Alkylation↗
PubMed2006

Cyclization reactions of homopropargyl azide derivatives catalyzed by PtCl4 in ethanol solution: synthesis of functionalized pyrrole derivatives.

[Structure: see text] PtCl4-catalyzed cyclization reactions of homopropargyl azide derivatives to pyrrole rings were investigated. Using ethanol as solvent with 2,6-di-tert-butyl-4-methylpyridine as the base was found to be the best set of conditions for effecting this ring-closing reaction. These reaction conditions can be applied to the preparation of functionalized pyrrole derivatives, with no effect on the functional groups.

Azides↗
PubMed2001

Effects of staurosporine, U-73122, wortmannin, 4-hydroxynonenal and sodium azide upon the release of secreted beta-amyloid precursor protein from human platelets in response to thrombin stimulation.

In the present study, the release of secreted beta-amyloid precursor protein (AbetaPPs) in response to thrombin stimulation in platelets has been investigated. Incubation of platelets with thrombin produced a concentration-dependent release of AbetaPPs with a concomitant reduction in the AbetaPP remaining in the lysates. The response to thrombin was not affected by pretreatment for 15 min with the phospholipase C inhibitor U-73122, with the protein kinase C inhibitor staurosporine, or with hydrogen peroxide (which at the concentrations used affects the phosphoinositide signalling system in human platelets). In contrast, pretreatment with wortmannin and sodium azide reduced the responses to thrombin. These data would suggest that thrombin may cause the release of AbetaPPs from human platelets via an activation of a phospholipase C-independent pathway. Thrombin-stimulated AbetaPPs release was also reduced by 4-hydroxynonenal. This finding, if it is a phenomenon also found for CNS cells, could be of relevance to the pathogenesis of Alzheimer's disease, given that an accumulation of 4-hydroxynonenal is found in this disease.

Aldehydes↗
PubMed2005

Cyclic GMP, sodium nitroprusside and sodium azide reduce aqueous humour formation in the isolated arterially perfused pig eye.

The effect of nitric oxide (NO) on aqueous humour formation (AHF) and intraocular pressure (IOP) was studied using NO donors, sodium azide (AZ) and sodium nitroprusside (SNP). Using the porcine arterially perfused eye preparation, drug effects on AHF and IOP were measured by fluorescein dilution and manometry, respectively. Perfusion pressure of the ocular vasculature was also monitored using digital pressure transducer and pen recorder. L-Arginine (1.0 mM), a precursor of NO, but not D-arginine (1.0 mM), the inactive analogue, produced a significant reduction in AHF (28.5%) and IOP (21.1%). L-NAME (L-nitro-L-arginine) (10-100 microM), an NO synthase inhibitor, had no effect on AHF and IOP. However, L-NAME (100 microM) completely reversed L-arginine's effect. AZ and SNP reduced the AHF and IOP dose-dependently. AZ at 100 nM, 1 and 10 microM reduced AHF by 26.0, 39.7 and 51.7% and IOP by 10.8, 17.3 and 24.0%, respectively. SNP at 1, 10 and 100 microM reduced the AHF by 6.0, 24.2 and 35.4% and IOP by 3.5, 9.5 and 15.5%, respectively. 8-pCPT-cGMP (8-para-chlorophenyl-thioguanosine-3',5'-cyclic guanosine monophosphate, 10 microM), a cGMP analogue, also reduced the AHF (34.9%) and IOP (15.9%). The effects of AZ and SNP on the AHF and IOP were blocked by a soluble guanylate cyclase inhibitor ODQ (10 microM), whereas ODQ alone or combined with 8-pCPT-cGMP had no effect on the AHF and IOP. None of the drugs had any significant effect on ocular vasculature. The reduction of the AHF and IOP in the arterially perfused pig eye by nitrovasodilators is likely to involve the NO-cGMP pathway.

Animals↗
PubMed1980

Identification of the subunits of bovine heart mitochondrial NADH dehydrogenase that are exposed to the phospholipid bilayer by photo-labelling with 5-iodonaphth-1-yl azide.

Mitochondrial NADH dehydrogenase may be isolated from bovine heart as a lipoprotein complex (Complex I or NADH-ubiquinone oxidoreductase). Polypeptide subunits that are exposed to the hydrophobic region of the phospholipid bilayer were identified by photolabelling with the hydrophobic probe, 5-[125I]iodonaphth-1-yl azide. Chaotropic resolution of the labelled enzyme showed that the hydrophilic flavoprotein and iron-protein fragments of the enzyme were not in contact with the phospholipid bilayer. When complex I that had been partially depleted of phospholipids was photolabelled, incorporation of radioactivity into certain polypeptides was increased, indicating either conformational changes in protein or preferential association of these polypeptides with residual cardiolipin. A model NADH dehydrogenase structure is proposed on the basis of these results and those obtained with hydrophilic probes by Smith & Ragan (1980) Biochem. J. 185, 315-326.

Affinity Labels↗
PubMed1984

Kinetic and e.p.r. studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase.

The kinetics of inhibition of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase by cyanide (CN-) and azide (N3-) ions have been investigated by using steady-state methods. Both anions show complex non-competitive-inhibition patterns with respect to ascorbate, suggestive of anion binding at two different sites on the oxidized enzyme. To further investigate this finding, e.p.r. titrations of CN- and N3- binding to the 63Cu-reconstituted enzyme were carried out. Addition of approx. 2 equiv. of CN- to copper elicits a new signal with g = 2.217, g = 2.025, A = 17.0 mT characteristic of a copper (II)-cyano complex. Simulations show that this signal accounts for half the copper (II) in the enzyme. The remainder of the enzyme-bound copper is expressed by a signal close to, but not identical with, that of native enzyme. Further addition of CN- induces a simultaneous decrease in intensity of both of these signals so that their 1:1 ratio is maintained. Binding of N3-, on the other hand, changes the e.p.r. spectrum to a form different from either that of the native or CN- -treated enzyme, and integrates to 100% of the copper in the enzyme (g = 2.252, g = 2.050, A = 16.5 mT). Resolved superhyperfine structure is apparent in the g region. N3- binding is also accompanied by the appearance of a broad charge-transfer band centred at 387 nm. Neither 9 nor 35 GHz e.p.r. spectra show evidence for more than one (non-interacting) species of Cu(II) in native enzyme and N3- derivatives. The binding and reactivity of CN-, on the other hand, argues against independent copper sites in the enzyme.

Ascorbic Acid↗
PubMed1997

Azide-sensitive thylakoid membrane insertion of chimeric cytochrome f polypeptides imported by isolated pea chloroplasts.

Post-translational integration of cytochrome f into thylakoid membranes was observed after import by isolated pea chloroplasts of a chimeric protein consisting of the presequence of the small subunit of ribulose 1,5-bisphosphate carboxylase fused to the cytochrome f precursor. Import of a similar chimeric protein lacking the C-terminal 33 amino acid residues resulted in a soluble cytochrome f protein in the thylakoid lumen, indicating that the C-terminal region contains a stop-transfer sequence for membrane integration. Azide inhibited the insertion of cytochrome f into the thylakoid membrane, whereas the ionophores nigericin and valinomycin had little effect on membrane insertion. The precursor of the 33 kDa protein, but not the 23 kDa protein, of the photo-system II oxygen-evolving complex inhibited the thylakoid insertion of cytochrome f, suggesting competition for a component of the transport pathway. These experiments suggest that the post-translational insertion of cytochrome f into the thylakoid membrane uses a SecA-dependent pathway.

Azides↗
PubMed2006

Metabolic regulation of in vitro-produced bovine embryos. II. Effects of phenazine ethosulfate, sodium azide and 2,4-dinitrophenol during post-compaction development on glucose metabolism and lipid accumulation.

The objective was to compare effects of three metabolic regulators on development of post-compaction bovine embryos. In-vitro-produced 8- to 16-cell embryos were allocated to treatments for 72 h in G2.2 medium as follows: 0.3 microm phenazine ethosulfate (PES); 27 microm sodium azide (NaN3); 30 microm 2,4-dinitrophenol (DNP); and control, no regulator. Treatments responded similarly for blastocyst rates and embryo quality responses (P > 0.1). The PES treatment resulted in higher glucose metabolism than the NaN3 treatment (18.5 v. 14.5 pmol per embryo per h, P < 0.05), and both did not differ from DNP or the control. The PES treatment tended to result in more flux of glucose through the pentose phosphate pathway (PPP) than the control (50.5 v. 21.5%, P < 0.11). The NaN3 treatment caused more glucose uptake than the PES treatment (38.9 v. 13.1 pmol per embryo per h, P < 0.01), but neither differed from the control or DNP treatment (P > 0.1). Glycolysis for the PES treatment was 187%, which was higher than any of the other groups (88-94%; P < 0.01). There were fewer medium + large lipid granules in the cytoplasm of PES-treated embryos than any other group, including the in vitro control (P < 0.01). However, in vivo control embryos had still fewer large and medium-sized lipid granules (P < 0.01) than the PES treatment. Developmental competence to Day 14 after embryo transfer was similar among treatments. The PES treatment increased glucose metabolism, tended to increase the PPP flux of glucose and clearly reduced accumulation of lipids in embryos produced in the chemically defined media used. Use of PES in culture media may be a promising approach to improving in vitro production of embryos.

2,4-Dinitrophenol↗
PubMed2001

Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation.

The introduction of chemically unique groups into proteins by means of non-natural amino acids has numerous applications in protein engineering and functional studies. One method to achieve this involves the utilization of a non-natural amino acid by the cell's native translational apparatus. Here we demonstrate that a methionine surrogate, azidohomoalanine, is activated by the methionyl-tRNA synthetase of Escherichia coli and replaces methionine in proteins expressed in methionine-depleted bacterial cultures. We further show that proteins containing azidohomoalanine can be selectively modified in the presence of other cellular proteins by means of Staudinger ligation with triarylphosphine reagents. Incorporation of azide-functionalized amino acids into proteins in vivo provides opportunities for protein modification under native conditions and selective labeling of proteins in the intracellular environment.

Animals↗
PubMed1998

ATP synthesis by F0F1-ATP synthase independent of noncatalytic nucleotide binding sites and insensitive to azide inhibition.

ATP hydrolyzing activity of a mutant alpha3beta3gamma subcomplex of F0F1-ATP synthase (DeltaNC) from the thermophilic Bacillus PS3, which lacked noncatalytic nucleotide binding sites, was inactivated completely soon after starting the reaction (Matsui, T., Muneyuki, E. , Honda, M., Allison, W. S., Dou, C., and Yoshida, M. (1997) J. Biol. Chem. 272, 8215-8221). This inactivation is caused by rapid accumulation of the "MgADP inhibited form" which, in the case of wild-type enzyme, would be relieved by ATP binding to noncatalytic sites. We reconstituted F0F1-ATP synthase into liposomes together with bacteriorhodopsin and measured illumination-driven ATP synthesis. Remarkably, DeltaNC F0F1-ATP synthase catalyzed continuous turnover of ATP synthesis while it could not promote ATP-driven proton translocation. ATP synthesis by DeltaNC F0F1-ATP synthase, as well as wild-type enzyme, proceeded even in the presence of azide, an inhibitor of ATP hydrolysis that stabilizes the MgADP inhibited form. The time course of ATP synthesis by DeltaNC F0F1-ATP synthase was linear, and gradual acceleration to the maximal rate, which was observed for the wild-type enzyme, was not seen. Thus, ATP synthesis can proceed without nucleotide binding to noncatalytic sites even though the rate is sub-maximal. These results indicate that the MgADP inhibited form is not produced in ATP synthesis reaction, and in this regard, ATP synthesis may not be a simple reversal of ATP hydrolysis.

Adenosine Triphosphate↗
PubMed1997

Structural studies by high-field NMR spectroscopy of a binary-addressed complementary oligonucleotide system juxtaposing pyrene and perfluoro-azide units.

Recently, a new approach has been proposed to improve the site-specificity and efficiency of the modification of nucleic acid target sequences, the binary system of complementary-addressing nucleic acid sequences. The binary system comprises two oligonucleotides, one modified with a photosensitizing group and the other with a photoreactive group. The sites of chemical modification are arranged to bring the two chemical functions close enough together in space to allow efficient energy transfer from the photo-excited photosensitizer to an arylazide moiety which expels N2 to form a nitrene which subsequently covalently labels the target nucleic acid. Structural analysis performed by high-resolution 2D NMR spectroscopy (400 MHz and 600 MHz) are reported for the model binary system 1:2:3, where 1 is the target 12-mer pdGTATCAGTTTCT, 2 is a photoactivatable fluoroazide derivative dAGAAACp-L-Az and 3 is the photosensitizer derivative Pyr-pdTGATAC (here: Az is the p-azidotetrafluorobenzyl group, Pyr the pyrenyl-1-methylamino group, L a linker group). The assignment of oligonucleotide and modifying group protons was performed using 1H COSY, TOCSY and NOESY experiments. Comprehensive analysis of 1H NOESY spectra of 1:2:3 showed that terminal fragments of the complex [5'p-1T-2G-3A-4T-], [-21A-22T-23A-24C], [-8T-9T-10T-11C-12T] and [13A-14G-15A-15A-17A-18C-] gave a continuous set of intra- and inter-nucleotide interactions, typical of regular double-stranded B-DNA. In contrast, the central region of the complex composed of 5C, 6A, 7G, 19T and 20G nucleotide residues, nearest the Pyr and Az groups, was found to be distorted. Thus some signals from aromatic and/or sugar-ring protons of the above nucleotide residues were extremely broadened or almost absent. Moreover, some intra- and/or inter-nucleotide interactions, typical of the regular DNA duplex, were not detected for the [-5C-6A-7G-] and [-19T-20G-] regions of the tandem system. Instead of that, some cross-peaks of low-intensity between the H2 proton of the Pyr group and 7G(H1'), 7G(H2'/H2"), 7G(H3'), 4T(H2"), 4T(H4') and 4T(H5'/H5") were observed. Additional 1H -1H NOE-interactions between methylene protons of the linker group L and some sugar ring protons of 18C nucleotide residue were detected. A preliminary structural model, constructed using proton-proton distances between Pyr and the DNA and Az-L and DNA obtained from a 1H NOESY experiment at 300 ms mixing time as constraints for the refinement of the structure, displayed significant distortion from B-DNA of the double-stranded helix in the middle of the complex, (-5C-6A-7G, -18C-19T-20G-). The Pyr group was located in what remains of the minor groove near 4T, 5C, 6A and 7G and the centroid of the azide ring less than 9A degrees from the centroid of the ring system of Pyr group.

Azides↗