Imidazole-rich copper peptides as catalysts in xenobiotic degradation.

Laccases, oxidative copper-enzymes found in fungi and bacteria were used as the basis in the design of nona- and tetrapeptides. Laccases are known to be excellent catalysts for the degradation of phenolic xenobiotic waste. However, since solvent extraction of laccases is environmentally-unfriendly and yields obtained are low, they are less preferred compared to synthetic catalysts.

Histidine-based copper tetrapeptides as enantioselective catalysts for aldol reactions.

Copper(ii)-peptides are widely used as industrial catalysts such as in the aerobic oxidation of organic molecules, formation of new C-H bonds and in the azide-alkyne cycloaddition reaction. The length of peptides and the effect of adding copper metal into peptides were questioned in their field of applications. Five novel histidine-based tetrapeptides with the sequences HAAD (P1), HAFD (P2), HAVD (P3), AGHD (P4) and PGHD (P5) were synthesized using the solid phase peptide scheme and analysed with high performance liquid chromatography (HPLC) and liquid chromatography-mass spectrometry (LC-MS) with percentage purities as high as 99.

Crystal structure of (Z)-4-methylbenzyl 3-[1-(5-methylpyridin-2-yl)ethylidene]dithiocarbazate.

In the title di-thio-carbazate compound, C17H19N3S2, the central CN2S2 residue is essentially planar (r.m.s.