B
Burkhard Bechinger
Researcher at University of Strasbourg
Publications - 123
Citations - 3996
Burkhard Bechinger is an academic researcher from University of Strasbourg. The author has contributed to research in topics: Membrane & Lipid bilayer. The author has an hindex of 32, co-authored 114 publications receiving 3234 citations. Previous affiliations of Burkhard Bechinger include Centre national de la recherche scientifique & Institut Universitaire de France.
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Journal ArticleDOI
Antimicrobial Peptides: Mechanisms of Action and Resistance:
TL;DR: Recent advances in understanding of the diverse mechanisms of action of cationic AMPs are described and the bacterial resistance against these peptides and the recently developed peptide GL13K is used as an example.
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Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice
Andreas Muhs,David T. Hickman,Maria Pihlgren,Nathalie Chuard,Valérie Giriens,Carine Meerschman,Ingrid Van der Auwera,Fred Van Leuven,Masae Sugawara,Marie-Catherine Weingertner,Burkhard Bechinger,Ruth Greferath,Nadine Kolonko,Luitgard Nagel-Steger,Detlev Riesner,Roscoe O. Brady,Andrea Pfeifer,Claude Nicolau +17 more
TL;DR: It is concluded that the association with liposomes induced a variation of the immunogenic structures and thereby different immunogenicities, implying that antibodies against amyloid sequences in the β-sheet conformation are preferred as potential therapeutic agents in Alzheimer's disease.
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Cationic amphipathic histidine-rich peptides for gene delivery.
TL;DR: The rationale that led to the development of LAH4 as a DNA carrier is described as well as the biophysical methods that have allowed us to propose a model which could explain the way this peptide destabilizes the endosomal bilayer.
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The membrane interactions of antimicrobial peptides revealed by solid-state NMR spectroscopy
TL;DR: Various solid-state NMR approaches are presented and the basic underlying concept how angular information can be obtained from oriented samples is developed and it is demonstrated how this information is used to calculate structures and topologies of peptides in their native liquid-disordered phospholipid bilayer environment.
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15N chemical shift referencing in solid state NMR.
TL;DR: (15)NH4Cl in its powdered form is a suitable external reference as it produces narrow lines when compared to other reference compounds and at the same time allows for the set-up of cross-polarization NMR experiments.