Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Torsten Wieprecht"'
Publikováno v:
Comptes Rendus Chimie. 10:326-340
Hydrogen peroxide based bleach reactions are increasingly important for many applications such as pulp and paper bleach, pre-treatment of cotton, waste water treatment and laundry. The search of catalysts being able to effectively activate peroxide i
Publikováno v:
Journal of Surfactants and Detergents. 7:59-66
Oxidation catalysis is one approach used to improve the performance of hydrogen peroxide in laundry bleach applications. We introduce herein a new class of bleach catalysts based on the ligand 2,2′∶6′,2″ terpyridine. A set of manganese comple
Publikováno v:
Journal of Molecular Catalysis A: Chemical. 203:113-128
The ability of manganese(II) complexes with substituted terpyridine (terpy) ligands to activate hydrogen peroxide and to catalyze oxidation of the substrates Morin and Trolox C was studied in aqueous alkaline solution. Introduction of π-donor substi
Publikováno v:
Biophysical Chemistry. 85:187-198
The thermodynamics of binding of the antibacterial peptide magainin 2 amide (M2a) to negatively charged small (SUVs) and large (LUVs) unilamellar vesicles has been studied with isothermal titration calorimetry (ITC) and CD spectroscopy at 45 degrees
Autor:
Torsten Wieprecht, Margitta Dathe
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1462:71-87
Antibacterial, membrane-lytic peptides belong to the innate immune system and host defense mechanism of a multitude of animals and plants. The largest group of peptide antibiotics comprises peptides which fold into an amphipathic α-helical conformat
Publikováno v:
Journal of Molecular Biology. 294:785-794
Amphipathic alpha-helices are the membrane binding motif in many proteins. The corresponding peptides are often random coil in solution but are folded into an alpha-helix upon interaction with the membrane. The energetics of this ubiquitous folding p
Publikováno v:
Biochemistry. 38:10377-10387
Magainins are positively charged amphiphatic peptides which permeabilize cell membranes and display antimicrobial activity. They are usually thought to bind specifically to anionic lipids, and binding studies have been performed almost exclusively wi
Publikováno v:
Journal of Chromatography A. 849:125-133
A promising approach in assessing hydrophobic peptide-membrane interactions is the use of reversed-phase high-performance liquid chromatography. The present study describes the preparation and properties of a noncovalent immobilized artificial membra
Autor:
M. Beyermann, E. Krause, W L Maloy, Richard M. Epand, M. Dathe, D L MacDonald, M. Bienert, Torsten Wieprecht
Publikováno v:
Biochemistry. 36:12869-12880
To investigate the influence of the angle subtended by the positively charged helix face on membrane activity, six amphipathic alpha-helical peptides with angles between 80 degrees and 180 degrees, but with retained hydrophobicity, hydrophobic moment
Autor:
D L MacDonald, W L Maloy, Eberhard Krause, Torsten Wieprecht, Michael Beyermann, Margitta Dathe, Bienert M
Publikováno v:
Biochemistry. 36:6124-6132
The magainins are antibacterial peptides from the skin of Xenopus laevis. They show a broad range of activity against prokaryotic cells but lyse eukaryotic cells poorly. To elucidate the influence of peptide hydrophobicity on membrane activity and se