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Stable commercial primary ammonium chlorides were combined with tertiary amines to initiate the controlled ring opening polymerisation of amino acid N-carboxyanhydrides to yield polypeptides with defined end group structure, predetermined molar mass and narrow molar mass distribution.

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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, 3190-70-3, name is (S)-4-Isobutyloxazolidine-2,5-dione, introducing its new discovery. Safety of (S)-4-Isobutyloxazolidine-2,5-dione

Antimicrobial peptides (AMPs), particularly those effective against methicillin-resistant Staphylococcus aureus (S. aureus) and antibiotic-resistant Pseudomonas aeruginosa (P. aeruginosa), are important alternatives to antibiotics. Typical peptide synthesis methods involving solid-phase sequential synthesis are slow and costly, which are obstacles to their more widespread application. In this paper, we synthesize peptides via ring-opening polymerization of alpha-amino acid N-carboxyanhydrides (NCA) using a transition metal initiator. This method offers high potential for inexpensive synthesis of substantial quantities of AMPs. Lysine (K) was chosen as the hydrophilic amino acid and alanine (A), phenylalanine (F), and leucine (L) as the hydrophobic amino acids. We synthesized five series of AMPs (i.e., P(KA), P(KL), P(KF), P(KAL), and P(KFL)), varied the hydrophobic amino acid content from 0 to 100%, and determined minimal inhibitory concentrations (MICs) against clinically important Gramnegative and Gram-positive bacteria and fungi (i.e., Escherichia coli (E. coli), P. aeruginosa, Serratia marcescens (S. marcescens), and Candida albicans (C. albicans). We found that P(K10F 7.5L7.5) and P(K10F15) show the broadest activity against all five pathogens and have the lowest MICs against these pathogens. For P(K10F7.5L7.5), the MICs against E. coli, P. aeruginosa, S. marcescens, S. aureus, and C. albicans are 31 mug/mL, 31 mug/mL, 250 mug/mL, 31 mug/mL, and 62.5 mug/mL, while for P(K10F15) the respective MICs are 31 mug/mL, 31 mug/mL, 250 mug/mL, 31 mug/mL, and 125 mug/mL. These are lower than the MICs of many naturally occurring AMPs. The membrane depolarization and SEM assays confirm that the mechanism of microbe killing by P(K10F 7.5L7.5) copeptide includes membrane disruption, which is likely to inhibit rapid induction of AMP-resistance in pathogens.

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Two novel soluble polymer-bound oligo-L-leucines 2 and 5, Which can be retained by a membrane reactor system, have been prepared and used as catalysts for the continuously operated asymmetric epoxidation of chalcone. The optimized batch reaction conditions yield epoxychalcone in high enantioselectivities (up to 94%) and conversions (over 99%) after 15 minutes.

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The invention relates to a process for the preparation of N-carboxyanhydrides by reaction of the corresponding amino acid with phosgene, diphosgene and/or triphosgene in a solvent medium, characterized in that the reaction is a least partially carried out in the presence of an unsaturated organic compound which has one or more ethylenic double bonds. The N-carboxyanhydrides are thus obtained with better yields and an improved purity.

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A porous, homochiral titanium-phosphonate material based on a tripodal peptide scaffold was used as a heterogeneous reaction medium for the enantioselective hydration (>99%) of styrene oxide. This titanium-phosphonate material, which was shown to contain confined chiral spaces, was prepared by polymerization of L-leucine onto a tris(2-aminoethyl)amine initiator, followed by capping with phosphonate groups and completed by non-aqueous condensation with titanium isopropoxide. Circular dichroism confirmed that the peptide tethers yielded a secondary structure. X-ray powder diffraction and transmission electron microscopy supported by a semi-empirical model showed the likely formation of a porous, lamellar material that was quantified by nitrogen adsorption.

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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, 3190-70-3, name is (S)-4-Isobutyloxazolidine-2,5-dione, introducing its new discovery. Recommanded Product: (S)-4-Isobutyloxazolidine-2,5-dione

A practical procedure has been developed for grafting poly(amino acid) on silica gel as an efficient and recoverable catalyst in the Julia-Colonna asymmetric epoxidation with high enantioselectivities. Separation and recovery of the catalyst of poly(amino acid) have been remarkably improved by grafting on silica gel without a significant loss of enantioselectivity and activity.

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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, 3190-70-3, name is (S)-4-Isobutyloxazolidine-2,5-dione, introducing its new discovery. Product Details of 3190-70-3

The Julia-Colonna asymmetric epoxidation reaction of substituted benzalacetophenone afforded the corresponding epoxide with high yield and high enantioselectivity, catalyzed by the specified length of poly-l-leucine (chain length n > 15). Poly-l-leucine catalysts have been prepared by the polymerization reaction of l-leucine-NCA with initiators (BnONa, n-BuNH2, H2O) and characterized by the MALD1-TOF Mass and IR analysis.

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A facile synthesis of N-carboxyanhydrides and poly(alpha-amino acid) using di-tert-butyltricarbonate (DBTC) is discussed. A one-pot synthesis of poly(amino acid) from an amino acid and DBTC as a dehydrating agent is also discussed. It is found that ring-opening polymerization of alpha-amino acid-N-carboxyanhydrides (NCA) is advantageous over the polycondensation because ring-opening polymerization, which is a chain polymerization is capable of providing polypeptides with precise topology. Results show that the system is suitable to synthesize NCA and poly(amino acid) from amino acids having acid-sensitive protecting groups.

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The recent advance of particle size engineering in nanometer ranges has widened the formulation opportunities of relatively water-insoluble drugs. However, the ‘nanoformulation’ suffers from a lack of systematic understanding about the requirements of polymeric stabilizers. Furthermore, the polymers that can be used for the preparation of nanocrystals are so limited that finding a proper stabilizer for a given formulation is often difficult. In this study, amino acid copolymers whose properties can systematically be tailored are developed, and their morphological and compositional effects are investigated. Copolymers containing lysine (K) as their hydrophilic segments, and phenylalanine (F) or leucine (L) as their hydrophobic segments successfully produce stable nanocrystals (200-300 nm) in water, while copolymers of K and alanine (A) could not generate nanosized particles. Not the morphology but the hydrophobicity of copolymers seems to be a critical parameter in the preparation of drug nanocrystals by wet comminution. The effective stabilization performance of copolymers requires the hydrophobic moiety content to be higher than 15 mol%. Comminution for only 5 min is long enough for nanocrystal preparation, and the crystallinity of drug is found intact after the processing.

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Amphiphilic block copolypeptides were prepared through transition-metal- mediated polymerization of amino acid N-carboxyanhydrides. In aqueous solution these materials form strong hydrogels at low concentrations. The self-assembly process that is responsible for gelation was investigated by measuring the rheological properties of the gels for a variety of molecular architectures: poly-L-lysine-&-poly-L-leucine diblock and poly-L-lysine-b-poly-L-leucine-b- poly-L-lysine triblock copolypeptides. Experiments showed that the rodlike helical secondary structure of enantionierically pure poly-L-leucine blocks was instrumental for gelation at polypeptide concentrations as low as 0.25 wt %. The hydrophilic polyelectrolyte segments have stretched coil configurations and stabilize the twisted fibril assemblies by forming a corona around the hydrophobic core. The self-assembly of hydrophobic blocks is highly specific and sensitive to the chirality of the helices. It was found that mechanical properties of the gels can be tuned through the molecular architecture of the block copolypeptides and also by carefully mixing different polypeptides in solution.

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