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The antibiotic feglymycin is a linear 13-mer peptide synthesized by the bacterium Streptomyces sp. DSM 11171. It mainly consists of the nonproteinogenic amino acids 4-hydroxyphenylglycine and 3,5-dihydroxyphenylglycine. An alanine scan of feglymycin was performed by solution-phase peptide synthesis in order to assess the significance of individual amino acid side chains for biological activity. Hence, 13 peptides were synthesized from di- and tripeptide building blocks, and subsequently tested for antibacterial activity against Staphylococcus aureus strains. Furthermore we tested the inhibition of peptidoglycan biosynthesis enzymes MurA and MurC, which are inhibited by feglymycin. Whereas the antibacterial activity is significantly based on the three amino acids D-Hpg1, L-Hpg5, and L-Phe12, the inhibitory activity against MurA and MurC depends mainly on L-Asp13. The difference in the position dependence for antibacterial activity and enzyme inhibition suggests multiple molecular targets in the modes of action of feglymycin. A la mode scanning: An alanine scan of the peptide antibiotic feglymycin was performed by solution-phase peptide synthesis to assess the significance of individual amino acid side chains for its biological activity. Antibacterial activity against Staphylococcus aureus and the inhibition of enzymes MurA and MurC depend on different amino acids.

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Pyridazine | C4H4N2636 – PubChem

 

Chemistry is an experimental science, and the best way to enjoy it and learn about it is performing experiments. Quality Control of 3-Phenyl-6-chloropyridazine. Introducing a new discovery about 20375-65-9, Name is 3-Phenyl-6-chloropyridazine

The 5-substituted 4-methoxycarbonyloxazole 5 derived from L-serine derivative 3 using diphenyl phosphorazidate (DPPA) has been converted to a 2,4-diaminosugar antibiotic, prumycin.

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The invention discloses a N – substituted pyrazolo [3, 4 – d] pyrimidine compound of preparation method and application. The compounds have the formula 1 illustrated structure, wherein R is a cyclic or non-cyclic aliphatic alkyl, heterocyclic group, acyl-containing groups, containing a hydroxy group, mercapto-containing group; R1 Is methoxy, halogen, trifluoromethyl, ethoxy, acetyl, cyano, nitro, N, N – dimethyl, methyl, benzyloxy, substituted or non-substituted amino, substituted guanidino, substituted or non-substituted phosphate group, substituted or non-substituted sulfonic acid, long-chain fatty alkyl, long-chain aliphatic amino; when R is cyclopentyl basetime, R1 is not a substituted or non-substituted amino. The invention is one class of structure of novel compound, and the compound to phosphodiesterase 9 type good inhibition effect, while at the same time possess antioxidant activity, can be used as a phosphodiesterase 9-type inhibitor to be applied to treatment of Alzheimer’s disease. Type 1. (by machine translation)

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Reference of 20375-65-9, Chemistry is the science of change. But why do chemical reactions take place? Why do chemicals react with each other? The answer is in thermodynamics and kinetics.In a document type is Article, and a compound is mentioned, 20375-65-9, 3-Phenyl-6-chloropyridazine, introducing its new discovery.

Our previous work revealed that two adjacent D-alpha-aminoxy acids could form two homochiral N-O turns, with the backbone folding into an extended helical structure (1.88-helix). Here, we report the conformational studies of linear peptides 3-6, which contain a D,L-alpha-aminoxy acid dimer segment. The NMR and X-ray analysis of 3 showed that it folded into a loop conformation with two heterochiral N-O turns. This loop segment can be used to constrain tetrapeptides 4 and 6 to form a reverse turn structure. 1H NMR dilution studies, DMSO-d6 addition studies, and 2D-NOESY data indicated that tetrapeptides 4 and 6 folded into reverse turn conformations featured by a head-to-tail 16-membered-ring intramolecular hydrogen bond. In contrast, tetrapeptide 5 with L-Ala instead of Gly or D-Ala as the N-terminal amino acid could not form the desired reverse turn structure for steric reasons. Quantum mechanics calculations showed that model pentamide 7, with the same substitution pattern of 4, adopted a novel reverse turn conformation featuring two heterochiral N-O turns (each of an 8-membered ring hydrogen bond), a cross-strand 16-membered ring hydrogen bond, and a 7-membered ring gamma-turn.

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Chemistry is an experimental science, and the best way to enjoy it and learn about it is performing experiments. Computed Properties of C10H7ClN2. Introducing a new discovery about 20375-65-9, Name is 3-Phenyl-6-chloropyridazine

An aspect of catalytic antibody research that receives little attention in the literature involves hapten systems that fail to elicit antibody catalysts despite a high affinity immune response and hapten designs that resemble those known to elicit catalysts. We have investigated a series of 12 phosphate and phosphonate haptens in a total of three animal systems. Dramatic and reproducible differences were observed in the catalytic activities of polyclonal antibodies elicited by the different haptens. A phosphate hapten with a phenyl ring on the side of the hapten opposite the linker elicited reproducibly high levels of polyclonal antibody catalytic activity. The other 11 haptens, most with benzyl groups on the side of the hapten opposite the linker, elicited immune responses in which catalytic activity was significantly weaker in terms of the level of observed catalytic activity, as well as frequency of elicited catalysts. Our results indicate that subtle features of transition state analogue hapten structure can have a dramatic and reproducible influence over the catalytic activity of elicited antibodies in related haptens. Whatever the explanation, subtle changes in mechanistic features due to altered leaving group ability/location or overall hapten flexibility, the comprehensive data presented here indicate that phenyl or 4-nitrophenyl leaving groups located opposite the hapten linker are to be preferred in order to elicit highly active antibody catalysts for acyl hydrolysis reactions. (C) 2000 Elsevier Science Ltd.

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In homogeneous catalysis, the catalyst is in the same phase as the reactant. The number of collisions between reactants and catalyst is at a maximum.In a patent, 20375-65-9, name is 3-Phenyl-6-chloropyridazine, introducing its new discovery. category: pyridazine

Heterospirocyclic 3-amino-2H-azirines with a tetrahydropyran (Thp), tetrahydrothiopyran (Tht), or N-protected piperidine (Pip) moiety are useful reagents for the preparation of peptides containing the corresponding six-membered heterocyclic 4-amino-4-carboxylic acid unit. In the present study, tripeptides of the type H-Asp-D-Ala-Xaa-OMe, where Xaa is the heterocyclic amino acid, were prepared according to the ‘azirine/oxazolone method’.

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Novel 3-methoxy-2-oxoazetidine derivatives, which are shown by the following formula STR1 wherein R1 is amino, acylated amino or protected amino, are of value as intermediates for the synthesis of useful compounds represented by the formula STR2 wherein R1 has the same meaning as defined above, as drugs in the treatment of bacterial infections.

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20375-65-9, Name is 3-Phenyl-6-chloropyridazine, belongs to pyridazine compound, is a common compound. Product Details of 20375-65-9In an article, once mentioned the new application about 20375-65-9.

SOLUTION SYNTHESIS OF N-METHYLATED PEPTIDES BY THE DIPHENYL PHOSPHINIC MIXED ANHYDRIDE PROCEDURE

A proton NMR method has been used to monitor racemisation during the coupling of N-methylated amino acids by the diphenylphosphinic mixed anhydride procedure.No racemisation was observed when urethane protection employed, but use of the benzoyl group led extensive racemisation.The reagent was subsequently used for the assembly of several extensively N-methylated peptides.

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In heterogeneous catalysis, the catalyst is in a different phase from the reactants. Recommanded Product: 20375-65-9, At least one of the reactants interacts with the solid surface in a physical process called adsorption in such a way. 20375-65-9, name is 3-Phenyl-6-chloropyridazine. In an article，Which mentioned a new discovery about 20375-65-9

Design of cell-permeable stapled peptides as HIV-1 integrase inhibitors

HIV-1 integrase (IN) catalyzes the integration of viral DNA into the host genome, involving several interactions with the viral and cellular proteins. We have previously identified peptide IN inhibitors derived from the alpha-helical regions along the dimeric interface of HIV-1 IN. Herein, we show that appropriate hydrocarbon stapling of these peptides to stabilize their helical structure remarkably improves the cell permeability, thus allowing inhibition of the HIV-1 replication in cell culture. Furthermore, the stabilized peptides inhibit the interaction of IN with the cellular cofactor LEDGF/p75. Cellular uptake of the stapled peptide was confirmed in four different cell lines using a fluorescein-labeled analogue. Given their enhanced potency and cell permeability, these stapled peptides can serve as not only lead IN inhibitors but also prototypical biochemical probes or “nanoneedles” for the elucidation of HIV-1 IN dimerization and host cofactor interactions within their native cellular environment.

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Conformational and spacial preferences for substrates of PepT1

The conformation at the first residue of dipeptide substrates for the peptide transporter PepT1 has been probed using constrained peptide analogues, and the active conformation has been identified. The Royal Society of Chemistry 2005.

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