Transient viscous response of the human cornea probed with the Surface Force Apparatus.

Knowledge of the biomechanical properties of the human cornea is crucial for understanding the development of corneal diseases and impact of surgical treatments (e.g., corneal laser surgery, corneal cross-linking). Using a Surface Force Apparatus we investigated the transient viscous response of the anterior cornea from donor human eyes compressed between macroscopic crossed cylinders. Corneal biomechanics was analyzed using linear viscoelastic theory and interpreted in the framework of a biphasic model of soft hydrated porous tissues, including a significant contribution from the pressurization and viscous flow of fluid within the corneal tissue. Time-resolved measurements of tissue deformation and careful determination of the relaxation time provided an elastic modulus in the range between 0.17 and 1.43 MPa, and fluid permeability of the order of 10-13 m4/(N∙s). The permeability decreased as the deformation was increased above a strain level of about 10%, indicating that the interstitial space between fibrils of the corneal stromal matrix was reduced under the effect of strong compression. This effect may play a major role in determining the observed rate-dependent non-linear stress-strain response of the anterior cornea, which underlies the shape and optical properties of the tissue.

Complexation and synergistic boundary lubrication of porcine gastric mucin and branched poly(ethyleneimine) in neutral aqueous solution.

Lubrication of soft polydimethylsiloxane (PDMS) elastomer interfaces was studied in aqueous mixtures of porcine gastric mucin (PGM) and branched polyethyleneimine (b-PEI) at neutral pH and various ionic strengths (0.1-1.0 M). While neither PGM nor b-PEI improved lubrication compared to polymer-free buffer solution, their mixtures produced a synergistic lubricating effect by reducing friction coefficients by nearly two orders of magnitude, especially at slow sliding speed in the boundary lubrication regime. An array of spectroscopic studies revealed that small cationic b-PEI molecules were able to strongly bind and penetrate into large anionic PGM molecules, producing an overall contraction of the randomly coiled PGM conformation. The interaction also affected the structure of the folded PGM protein terminals, decreased the surface potential and increased light absorbance in PGM:b-PEI mixtures. Adding an electrolyte (NaCl) weakened the aggregation between PGM and b-PEI, and degraded the lubrication synergy, indicating that electrostatic interactions drive PGM:b-PEI complexation.

Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins.

Interfacial water constitutes a formidable barrier to strong surface bonding, hampering the development of water-resistant synthetic adhesives. Notwithstanding this obstacle, the Asian green mussel Perna viridis attaches firmly to underwater surfaces via a proteinaceous secretion (byssus). Extending beyond the currently known design principles of mussel adhesion, here we elucidate the precise time-regulated secretion of P. viridis mussel adhesive proteins. The vanguard 3,4-dihydroxy-L-phenylalanine (Dopa)-rich protein Pvfp-5 acts as an adhesive primer, overcoming repulsive hydration forces by displacing surface-bound water and generating strong surface adhesion. Using homology modelling and molecular dynamics simulations, we find that all mussel adhesive proteins are largely unordered, with Pvfp-5 adopting a disordered structure and elongated conformation whereby all Dopa residues reside on the protein surface. Time-regulated secretion and structural disorder of mussel adhesive proteins appear essential for optimizing extended nonspecific surface interactions and byssus' assembly. Our findings reveal molecular-scale principles to help the development of wet-resistant adhesives.

Molecular Structure and Equilibrium Forces of Bovine Submaxillary Mucin Adsorbed at a Solid-Liquid Interface.

By combining dynamic light scattering, circular dichroism spectroscopy, atomic force microscopy, and surface force apparatus, the conformation of bovine submaxillary mucin in dilute solution and nanomechanical properties of mucin layers adsorbed on mica have been investigated. The samples were prepared by additional chromatographic purification of commercially available products. The mucin molecule was found to have a z-average hydrodynamic diameter of ca. 35 nm in phosphate buffered solution, without any particular secondary or tertiary structure. The contour length of the mucin is larger than, yet of the same order of magnitude as the diameter, indicating that the molecule can be modeled as a relatively rigid polymeric chain due to the large persistence length of the central glycosylated domain. Mucin molecules adsorbed abundantly onto mica from saline buffer, generating polymer-like, long-ranged, repulsive, and nonhysteretic forces upon compression of the adsorbed layers. Detailed analysis of such forces suggests that adsorbed mucins had an elongated conformation favored by the stiffness of the central domain. Acidification of aqueous media was chosen as means to reduce mucin-mucin and mucin-substrate electrostatic interactions. The hydrodynamic diameter in solution did not significantly change when the pH was lowered, showing that the large persistence length of the mucin molecule is due to steric hindrance between sugar chains, rather than electrostatic interactions. Remarkably, the force generated by an adsorbed layer with a fixed surface coverage also remained unaltered upon acidification. This observation can be linked to the surface-protective, pH-resistant role of bovine submaxillary mucin in the variable environmental conditions of the oral cavity.