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Colloidal particles can bind to fluid interfaces with a capillary energy that is thousands of times the thermal energy. This phenomenon offers an effective route to emulsion and foam stabilization where the stability is influenced by the phase behavior of the particle-laden interface under deformation. Despite the vast interest in particle-laden interfaces, the key factors that determine the collapse of such an interface under compression have remained relatively unexplored. In this study, we illustrate the significance of the particle surface wettability and presence of electrolyte in the subphase on interparticle interactions at the interface and the resulting collapse mode. Various collapse mechanisms including buckling, particle expulsion, and multilayer formation are reported and interpreted in terms of particle-particle and particle-interface interactions.

The development of microbubbles toward functional, "theranostic" particles requires the incorporation of constituents with high binding specificity and therapeutic efficacy. Integrating peptides or proteins into the shell of lipid-based microbubbles can provide a means to access both receptor-ligand interactions and therapeutic properties. Simultaneously, peptides or proteins can define the characteristic monolayer mechanics of lipid bubbles and eliminate the need for post-bubble generation modification. The ability to engineer peptide sequences de novo that effectively partition into the bubble monolayer remains parametrically daunting. This work contributes to this effort using two simple amphipathic helical peptides that examine the role of local electrostatics and secondary structure. The two periodically sequenced peptides both have three positive charges, but peptide "K-2.5" spaces those charges 2.5 amino acids apart, while peptide "K-6.0" spaces the charges six amino acids apart. Size populations were determined for bubbles containing each peptide species using light scattering, and a quantitative method was developed to clearly define the fraction of peptides binding onto the microbubble monolayer. The impact of both the initial peptide concentration and the zwitterionic:anionic lipid ratio on peptide binding was also evaluated. Our results indicate that the lipid ratio affected only K-6.0 binding, which appears to be an outcome of the greater ensemble average α-helical population of the K-6.0. These findings provide further insights into the role of charge separation on peptide secondary structure, establishing a simple design metric for peptide binding onto microbubble systems.

The strict requirement of constructing a native lipid environment to preserve the structure and functionality of membrane proteins is the starting constraint when building biomaterials and sensor systems from these biomolecules. To enhance the viability of supported biomembranes systems and build new ligand display interfaces, we apply rationally designed peptides partitioned into the lipid bilayer interface. Peptides designed to form membrane-spanning α-helical anchoring domains are synthesized using solid-phase peptide synthesis. K(3)A(4)L(2)A(7)L(2)A(3)K(2)-FITC is synthesized on the 100 mg scale for use as a biomembrane anchoring molecule, where orthogonal side-chain modifications allow us to introduce probes enabling peptide localization within supported bilayers. The peptides are found to form α-helical domains within liposomes as assessed with circular dichroism spectroscopy. These peptides are designed to be incorporated into lipid bilayers supported by microspheres and serve as biomembrane anchoring moieties to amino-terminated surfaces. Here, the silica bead surface (4.7 μm diameter) is activated with homobifunctional NHS-PEG(3000)-NHS as "polymer cushion" spacers. This tethering to a subset of the K(3)A(4)L(2)A(7)L(2)A(3)K(2)-FITC molecules present in the bilayer is achieved by the fusion of liposomes followed by coupling of the peptide amino groups to the NHS presented from the silica microsphere surfaces. The biomembrane distributions of tethered and untethered K(3)A(4)L(2)A(7)L(2)A(3)K(2)-FITC are probed with confocal microscopy and are found to give 3D reconstructions consistent with largely homogeneous supported biomembranes. The fluidity of the untethered fraction of peptides within supported membranes is quantified using the fluorescence recovery after photobleaching (FRAP) technique. The presence of the PEG(3000) polymer cushion facilitated a 28.9% increase in peptide diffusivity over untethered bilayers at the lowest peptide to lipid ratio we examined. We show that rationally designed peptide-based anchors can be used to tether lipid bilayers, creating a polymer-cushioned lipid microenvironment on surfaces with high lateral mobility and facilitating the development of a new platform for ligand displays.

We describe a rationally designed peptide with tunable surface activity, where the dynamics of surface activity are an outcome of helical folding. Our rationally designed model peptide is surface-active only as an alpha-helix. We apply circular dichroism to show that the folded population can be controlled with changes in electrolyte concentration, and we apply pendant bubble tensiometry to explore dynamic surfactant activity. This study shows a peptide that responds to environmental stimuli with dynamic folding and surface activity. Extending this concept to selective binding peptides will lead to new tools, where dynamic surface activity is coupled to targeted binding.