Interactions between the Cell Membrane Repair Protein S100A10 and Phospholipid Monolayers and Bilayers.

Protein S100A10 participates in different cellular mechanisms and has different functions, especially at the membrane. Among those, it forms a ternary complex with annexin A2 and the C-terminal of AHNAK and then joins the dysferlin membrane repair complex. Together, they act as a platform enabling membrane repair. Both AHNAK and annexin A2 have been shown to have membrane binding properties. However, the membrane binding abilities of S100A10 are not clear. In this paper, we aimed to study the membrane binding of S100A10 in order to better understand its role in the cell membrane repair process. S100A10 was overexpressed by E. coli and purified by affinity chromatography. Using a Langmuir monolayer as a model membrane, the binding parameters and ellipsometric angles of the purified S100A10 were measured using surface tensiometry and ellipsometry, respectively. Phosphorus-31 solid-state nuclear magnetic resonance spectroscopy was also used to study the interaction of S100A10 with lipid bilayers. In the presence of a lipid monolayer, S100A10 preferentially interacts with unsaturated phospholipids. In addition, its behavior in the presence of a bilayer model suggests that S100A10 interacts more with the negatively charged polar head groups than the zwitterionic ones. This work offers new insights on the binding of S100A10 to different phospholipids and advances our understanding of the parameters influencing its membrane behavior.

Strong Headgroup Interactions Drive Highly Directional Growth and Unusual Phase Co-Existence in Self-Assembled Phenolic Films.

Self-assembled materials as surface coatings are used to confer functional properties to substrates, but such properties are highly dependent on molecular organization that can be controlled through tailoring the noncovalent interactions. For monomolecular films, it is well-known that strong, dipolar interactions can oppose line tension generating noncircular domain growth. While many surfactant films exhibit liquid crystalline arrangement of the alkyl chains, there are relatively few reports of crystalline headgroups. Here, we report the self-assembly of phenolic surfactants where the combination of hydrogen bonding and π-stacking leads to a herringbone arrangement of the headgroups, generating a molecular super-lattice that can be observed using grazing incidence X-ray diffraction; such an arrangement has been previously proposed for related phenolic systems but never experimentally observed. We also investigated using pH to modulate the intermolecular interactions and the response of the system in terms of molecular organization. The first hydroxyl deprotonation does not appear to impact the structure but has significant impact on the domain size and morphology. Higher pH generates both strong directional domain growth and a loss of the molecular lattice structure, attributed to a second deprotonation. In contrast, a shorter chain surfactant, lauryl gallate, forms a liquid expanded phase that can contract upon deprotonation. In the condensed phase, the deprotonation kinetics are unusually slow for which an internal charge re-organization is proposed. The slow kinetics leads to the co-existence of three distinct phases for a single component system over relatively long timescales and provides evidence of a liquid-mediated polymorphic transformation process in two-dimensional, soft-matter films. This work has implications for understanding the long-range ordering in aromatic self-assembled structures and the mechanisms underlying Langmuir monolayer polymorphism.

Model Lung Surfactant Films: Why Composition Matters.

Lung surfactant replacement therapies, Survanta and Infasurf, and two lipid-only systems both containing saturated and unsaturated phospholipids and one containing additional palmitic acid were used to study the impact of buffered saline on the surface activity, morphology, rheology, and structure of Langmuir monolayer model membranes. Isotherms and Brewster angle microscopy show that buffered saline subphases induce a film expansion, except when the cationic protein, SP-B, is present in sufficient quantities to already screen electrostatic repulsion, thus limiting the effect of changing pH and adding counterions. Grazing incidence X-ray diffraction results indicate an expansion not only of the liquid expanded phase but also an expansion of the lattice of the condensed phase. The film expansion corresponded in all cases with a significant reduction in the viscosity and elasticity of the films. The viscoelastic parameters are dominated by liquid expanded phase properties and do not appear to be dependent on the structure of the condensed phase domains in a phase separated film. The results highlight that the choice of subphase and film composition is important for meaningful interpretations of measurements using model systems.