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Moenomycin A is an amphiphilic phosphoglycolipid antibiotic that interferes with the transglycosylation step in peptidoglycan biosynthesis. The antibiotic consists of a branched pentasaccharide moiety, connected to the moenocinol lipid via a glycerophosphate linker. We have previously described the selection of aptamers that require the lipid group and the disaccharide epitopes of the oligosaccharide moiety for moenomycin binding. Here we report that the enriched moenomycin-binding library contains sequences that evolved for specific recognition of the unpolar lipid group of the antibiotic. These results suggest that the evolution of hydrophobic binding pockets in RNA molecules may be much more common than previously assumed.

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In principle PP meshes following an uncomplicated ventral hernia repair do not shrink at all. A moderate shrinkage in isolated cases might occur following heavyweight mesh implantation. Under controlled conditions recurrence as well as complication rates are equal for heavyweight and lightweight PP meshes. Quality of life improves up to 2 years following mesh repair with a trend to a better outcome for lightweight meshes. Pain and mobility scores reached standard values 12 months postoperatively without significant differences between the lightweight and heavyweight meshes.