For an insect to be able to efficiently attach to surfaces, the adhesive pads on the distal parts of its legs must establish large contact areas. In case of hairy adhesive pads this requires flexibility of the contact-forming bristles, called adhesive tarsal setae. However, too flexible setae would have a low mechanical stability resulting in a decreased attachment ability of the pads. Here we show that the adhesive tarsal setae of the ladybird beetle Coccinella septempunctata feature pronounced gradients in the material composition and properties along their length. The Young's modulus ranges from 1.2 MPa at the tips, where we found the incorporation of high proportions of the elastic protein resilin, to 6.8 GPa at the bases of the setae. These gradients likely represent an evolutionary optimization, which increases the performance of the adhesive system by enabling effective adaptation to rough surfaces while simultaneously preventing lateral collapse of the setae.

The morphology of the toe epithelium of the rock frog, Staurois parvus (Family Ranidae), was investigated using a variety of microscopical techniques. The toe pad epithelium is stratified (four to five cell layers), the apical parts of the cells of the outermost layer being separated by fluid-filled channels. The surface of these cells is covered by a dense array of nanopillars, which also cover the surface of subarticular tubercles and unspecialized ventral epithelium of the toes, but not the dorsal epithelium. The apical portions of the outer two layers contain fibrils that originate from the nanopillars and are oriented approximately normal to the surface. This structure is similar to the pad structure of tree frogs of the families Hylidae and Rhacophoridae, indicating evolutionary convergence and a common evolutionary design for reversible attachment in climbing frogs. The main adaptation to the torrent habitat seems to be the straightness of the channels crossing the toe pad, which will assist in drainage of excess water. The presence of nanopillar arrays on all ventral surfaces of the toes resembles that on clingfish suckers and may be a specific adaptation for underwater adhesion and friction. The relevance of these findings to the development of new biomimetically inspired reversible adhesives is discussed.

SummaryUnspecific adhesion of bacteria is usually the first step in the formation of biofilms on abiotic surfaces, yet it is unclear up to now which forces are governing this process. Alongside long-ranged van der Waals and electrostatic forces, short-ranged hydrophobic interaction plays an important role. To characterize the forces involved during approach and retraction of an individual bacterium to and from a surface, single cell force spectroscopy is applied: A single cell of the apathogenic species Staphylococcus carnosus isolate TM300 is used as bacterial probe. With the exact same bacterium, hydrophobic and hydrophilic surfaces can be probed and compared. We find that as far as 50 nm from the surface, attractive forces can already be recorded, an indication of the involvement of long-ranged forces. Yet, comparing the surfaces of different surface energy, our results corroborate the model that large, bacterial cell wall proteins are responsible for adhesion, and that their interplay with the short-ranged hydrophobic interaction of the involved surfaces is mainly responsible for adhesion. The ostensibly long range of the attraction is a result of the large size of the cell wall proteins, searching for contact via hydrophobic interaction. The model also explains the strong (weak) adhesion of S. carnosus to hydrophobic (hydrophilic) surfaces.

The adhesion of pathogenic bacteria to surfaces is of immense importance for health care applications. Via a combined experimental and computational approach, we studied the initiation of contact in the adhesion process of the pathogenic bacterium Staphylococcus aureus. AFM force spectroscopy with single cell bacterial probes paired with Monte Carlo simulations enabled an unprecedented molecular investigation of the contact formation. Our results reveal that bacteria attach to a surface over distances far beyond the range of classical surface forces via stochastic binding of thermally fluctuating cell wall proteins. Thereby, the bacteria are pulled into close contact with the surface as consecutive proteins of different stiffnesses attach. This mechanism greatly enhances the attachment capability of S. aureus. It, however, can be manipulated by enzymatically/chemically modifying the cell wall proteins to block their consecutive binding. Our study furthermore reveals that fluctuations in protein density and structure are much more relevant than the exact form of the binding potential.