First total synthesis of hoshinoamide A

Hoshinoamides A, B and C, linear lipopeptides, were isolated from the marine cyanobacterium Caldora penicillata, with potent antiplasmodial activity against chloroquine-sensitive Plasmodium falciparum. Herein, we describe the first total synthesis of hoshinoamide A by the combination of liquid-phase and solid-phase peptide synthesis. Liquid-phase synthesis is to improve the coupling yield of ʟ-Val3 and N-Me-ᴅ-Phe2. Connecting other amino acids efficiency and convergence is achieved by solid-state synthesis. Our synthetic strategy could synthesize the target peptide in high yield with good purity

First Total Synthesis of Hoshinoamides A

Hoshinoamides A, B and C, linear lipopeptides, were isolated from the marine cyanobacterium Caldora penicillata, with potent antiplasmodial activity against chloroquine-sensitive Plasmodium falciparum. Herein, we describe the first total synthesis of Hoshinoamides A. Our synthetic strategy uses the combined methods of solution and solid phase peptide synthesis. Liquid phase synthesis is to improve the coupling yield of L-Val3 and N-Me-D-Phe2. Connecting other amino acids efficiency and convergence by solid state synthesis. This synthetic strategy has good purity and high yield.

Iron Pincer Complexes as Catalysts in Cross-coupling of Aryl Halides and Phenylboronic Acid

Pincer complexes with iron as active metal center were synthesized to study their catalytic activity in Suzuki-Miyaura coupling reactions. Tridentate pincer ligand was synthesized by the reaction of diphenylchlorophosphine with m-aminophenol and m-phenylenediamine respectively in a 2:1 ratio in the presence of triethylamine as a base and tetrahydrofuran as solvent media. The resultant ligand was complexed with FeSO4 to obtain PCP complexes, C-1 with O and N atoms in the side arms and C-2 with both N atoms in the side arms. The synthesized complexes were examined for their C-C coupling efficiency in cross-coupling between phenyl boronic acid and para substituted halobenzenes. The research study aims to provide an alternative approach to the Pd catalyzed cross coupling methods, an otherwise subjugated method to obtain cross-coupled products. Also the study implores on the effect of variation in the side arm atom relating to the donating ability of the ligand and thereby relatively affecting the coupling yield of the catalysts.

Land for Food & Land for Nature?

Opinions on how to limit the immense impact of agriculture on wild species are divided. Some think it best to retain as much wildlife as possible on farms, even at the cost of lowering yield (production per unit area). Others advocate the opposite: increasing yield so as to limit the area needed for farming, and then retaining larger areas under natural habitats. Still others support a mixture of the two extremes, or an intermediate approach. Here we summarize a model designed to resolve this disagreement, and review the empirical evidence available to date. We conclude that this evidence largely supports the second, so-called land-sparing approach to reconciling agriculture and biodiversity conservation, but that important questions remain over the generality of these findings for different biota and for ecosystem services, how best to increase yields while limiting environmental externalities, and whether there are effective, socially just, and practical mechanisms for coupling yield growth to habitat retention and restoration.

Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier

This paper describes the covalent immobilization of penicillin G acylase from Escherichia coli on sepabeads EC-EP, an epoxy-activated polymethacrylic carrier and kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillins and semi-synthetic ?-lactam antibiotics synthesis reactions. About 2.7 mg of the pure enzyme was immobilized onto each gram of sepabeads with an enzyme coupling yield of 96.9%. However, it seems that the activity coupling yield is not correlated with the amount of enzyme bound and the maximum yield of 89.4% can be achieved working at low enzyme loading (0.14 mg g-1). Immobilization of the penicillin acylase resulted in slightly different pH activity profile and temperature optima, indicating that the immobilization by this method imparted structural and conformational stability of this enzyme. It appears that both free and immobilized penicillin acylase followed simple Michaelis-Menten kinetics, implying the same reaction mechanism in both systems.

ISOTOPE SHIFT OF THE ENERGY GAP OF DIAMOND

Optical absorption and cathodoluminescence measurements show that the indirect energy gap of 13 C diamond is 13.6±0.2 meV larger than for 12 C diamond. Calculations based on the measured shift of the energy gap with temperature, allowing only for changes in electron-phonon coupling, yield a value for the isotope shift of 13.5±2.0 meV , in excellent agreement with experiment.