The Antimicrobial peptides (e.g. defensins, hevein-like molecules and food-protecting peptides like nisin) are
able to interact specifically with contact structures on pathogen surfaces. Besides protein receptors, important recognition
points for such contacts are provided by pathogen glycan chains or surface lipids. Therefore, structural data concerning
surface exposed glycans and lipids are of the highest clinical interest since these recognition functions play a key role
when optimising anti-infection therapies. Approaches in nanomedicine and nanopharmacology in which various biophysical
techniques such as NMR (Nuclear Magnetic Resonance), AFM (Atomic Force Microscopy), SPR (Surface Plasmon
Resonance) and X-ray crystallography can be combined with biochemical and cell-biological methods will lead to improved
antimicrobial peptides by this rational drug design approach. Such a strategy is extremely well suited to support
clinical studies focussing on an effective fight against multiresistant pathogens. The data sets which are described here can
be considered as universal for the design of various antimicrobial drugs against certain pathogens (bacteria, viruses and
fungi) which cause severe diseases in humans and animals. Furthermore, these insights are also helpful for progressing
developments in the field of food conservation and food preservation. A detailed analysis of the structure-function relationships
between antimicrobial peptides and contact molecules on pathogen surfaces at the sub-molecular level will lead
to a higher degree of specificity of antimicrobial peptides.
Keywords: Biophysical methods, Nanomedicine, Nanopharmacology, Structure-function relationship.
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