The occurrence and spreading of multidrug resistance in bacterial pathogens represent one of the greatest challenges of the 21st century. With fewer and fewer new antibiotics in development, novel and unconventional concepts in drug development and formulation need to be explored to overcome the global antibiotics crisis. Biomedical nanotechnology offers promising strategies for the reformulation of established antibiotics in such a way that they regain their activity against resistant pathogens. Herein, promising developments aimed at the synthesis of potent nanoparticle‐based formulations of glycopeptide antibiotics are reviewed. While glycopeptide antibiotics such as vancomycin and teicoplanin are widely used as drugs of last resort against Gram‐positive pathogens such as methicillin‐resistant Staphylococcus aureus (MRSA), bacterial resistance against these drugs is spreading. However, inhibiting cell wall synthesis via binding to cell wall precursor peptidoglycans, glycopeptide antibiotics exhibit a unique mode of action that renders them particularly promising candidates for nanoparticle‐based formulations with the ability to overcome glycopeptide antibiotic resistance. Herein, different formulation concepts based on multivalent presentation and encapsulation are introduced, different synthesis and conjugation strategies are discussed, and an attempt is made to rationalize their effects on the antibacterial activity of the resulting nanoparticle formulations.

In many applications such as diagnostics and therapy development, small peptide fragments consisting of only a few amino acids are often attractive alternatives to bulky proteins. This is due to...

The influence of nanoscale surface topography on protein adsorption is highly important for numerous applications in medicine and technology. Herein, ferritin adsorption at flat and nanofaceted, single-crystalline Al2O3 surfaces is investigated using atomic force microscopy and X-ray photoelectron spectroscopy. The nanofaceted surfaces are generated by the thermal annealing of Al2O3 wafers at temperatures above 1000 °C, which leads to the formation of faceted saw-tooth-like surface topographies with periodicities of about 160 nm and amplitudes of about 15 nm. Ferritin adsorption at these nanofaceted surfaces is notably suppressed compared to the flat surface at a concentration of 10 mg/mL, which is attributed to lower adsorption affinities of the newly formed facets. Consequently, adsorption is restricted mostly to the pattern grooves, where the proteins can maximize their contact area with the surface. However, this effect depends on the protein concentration, with an inverse trend being observed at 30 mg/mL. Furthermore, different ferritin adsorption behavior is observed at topographically similar nanofacet patterns fabricated at different annealing temperatures and attributed to different step and kink densities. These results demonstrate that while protein adsorption at solid surfaces can be notably affected by nanofacet patterns, fine-tuning protein adsorption in this way requires the precise control of facet properties.

DNA origami nanostructures have emerged as functional materials for applications in various areas of science and technology. In particular, the transfer of the DNA origami shape into inorganic materials using...