The structure of water near non-polar molecular fragments or surfaces mediates the hydrophobic interactions that underlie a broad range of interfacial, colloidal and biophysical phenomena. Substantial progress over the past decade has improved our understanding of hydrophobic interactions in simple model systems, but most biologically and technologically relevant structures contain non-polar domains in close proximity to polar and charged functional groups. Theories and simulations exploring such nanometre-scale chemical heterogeneity find it can have an important effect, but the influence of this heterogeneity on hydrophobic interactions has not been tested experimentally. Here we report chemical force microscopy measurements on alkyl-functionalized surfaces that reveal a dramatic change in the surfaces' hydrophobic interaction strengths on co-immobilization of amine or guanidine groups. Protonation of amine groups doubles the strength of hydrophobic interactions, and guanidinium groups eliminate measurable hydrophobic interactions in all pH ranges investigated. We see these divergent effects of proximally immobilized cations also in single-molecule measurements on conformationally stable β-peptides with non-polar subunits located one nanometre from either amine- or guanidine-bearing subunits. Our results demonstrate the importance of nanometre-scale chemical heterogeneity, with hydrophobicity not an intrinsic property of any given non-polar domain but strongly modulated by functional groups located as far away as one nanometre. The judicious placing of charged groups near hydrophobic domains thus provides a strategy for tuning hydrophobic driving forces to optimize molecular recognition or self-assembly processes.

Oligomers of β-amino acids ("β-peptides") can be designed to fold into stable helices that display side chains with a diverse range of chemical functionality in precise arrangements. We sought to determine whether the predictable, three-dimensional side-chain patterns generated by β-peptides could be used in combination with single-molecule force spectroscopy to quantify how changes in nanometer-scale chemical patterns affect intermolecular interactions. To this end, we synthesized β-peptides that were designed to be either globally amphiphilic (GA), i.e., display a global segregation of side chains bearing hydrophobic and cationic functional groups, or non-globally amphiphilic (iso-GA), i.e., display a more uniform distribution of hydrophobic and cationic functional groups in three-dimensions. Single-molecule force measurements of β-peptide interactions with hydrophobic surfaces through aqueous solution (triethanolamine buffer, pH 7.2) reveal that the GA and iso-GA isomers give rise to qualitatively different adhesion force histograms. The data are consistent with the display of a substantial nonpolar domain by the GA oligomer, which leads to strong hydrophobic interactions, and the absence of a comparable domain on the iso-GA oligomer. This interpretation is supported by force measurements in the presence of methanol, which is known to disrupt hydrophobic interactions. Our ability to associate changes in measured forces with changes in three-dimensional chemical nanopatterns projected from conformationally stable β-peptide helices highlights a contrast between this system and conventional peptides (α-amino acid residues): conventional peptides are more conformationally flexible, which leads to uncertainty in the three-dimensional nanoscopic chemical patterns that underlie measured forces. Overall, we conclude that β-peptide oligomers provide a versatile platform for quantifying intermolecular interactions that arise from specific functional group nanopatterns.

We report colloidally stable emulsions of thermotropic liquid crystals (LCs) that can detect the presence of amphiphilic analytes in aqueous environments. Our approach makes use of a Pickering stabilization strategy consisting of surfactant–nanoparticle complexes (SiO2/C n TAB, n = 8, 12, 16) that adsorb to aqueous/LC droplet interfaces. This strategy can stabilize LC emulsions against coalescence for at least 3 months. These stabilized LC emulsions also retain the ability to respond to the presence of model anionic, cationic, and nonionic amphiphiles (e.g., SDS, C12TAB, C12E4) in aqueous solutions by undergoing “bipolar-to-radial” changes in LC droplet configurations that can be readily observed and quantified using polarized light microscopy. Our results reveal these ordering transitions to depend upon the length of the hydrocarbon tail of the C n TAB surfactant used to form the stabilizing complexes. In general, increasing C n TAB surfactant tail length leads to droplets that respond at lower analyte concentrations, demonstrating that this Pickering stabilization strategy can be used to tune the sensitivities of the stabilized LC droplets. Finally, we demonstrate that these colloidally stable LC droplets can report the presence of rhamnolipid, a biosurfactant produced by the bacterial pathogen Pseudomonas aeruginosa. Overall, our results demonstrate that this Pickering stabilization strategy provides a useful tool for the design of LC droplet-based sensors with substantially improved colloidal stability and new strategies to tune their sensitivities. These advances could increase the potential practical utility of these responsive soft materials as platforms for the detection and reporting of chemical and biological analytes.

We report an investigation of the adhesive force generated between the hydrophobic tip of an atomic force microscope (AFM) and surfaces presenting oligopeptides immobilized using either short (∼1 nm) or long (∼60 nm) tethers. Specifically, we used either sulfosuccinimidyl-4-(N-maleimidomethyl)cyclohexane-1-carboxylate (SSMCC) or 10 kDa polyethylene glycol (PEG) end-functionalized with maleimide and N-hydroxysuccinimide groups to immobilize helical oligomers of β-amino acids (β-peptides) to mixed monolayers presenting tetraethylene glycol (EG4) and amine-terminated EG4 (EG4N) groups. When SSMCC was used to immobilize the β-peptides, we measured the adhesive interaction between the AFM tip and surface to rupture through a single event with magnitude consistent with the interaction of a single β-peptide with the AFM tip. Surprisingly, this occurred even when, on average, multiple β-peptides were located within the interaction area between the AFM tip and surface. In contrast, when using the long 10 kDa PEG tether, we observed the magnitude of the adhesive interaction as well as the dynamics of the rupture events to unmask the presence of the multiple β-peptides within the interaction area. To provide insight into these observations, we formulated a simple mechanical model of the interaction of the AFM tip with the immobilized β-peptides and used the model to demonstrate that adhesion measurements performed using short tethers (but not long tethers) are dominated by the interaction of single β-peptides because (i) the mechanical properties of the short tether are highly nonlinear, thus causing one β-peptide to dominate the adhesion force at the point of rupture, and (ii) the AFM cantilever is mechanically unstable following the rupture of the adhesive interaction with a single β-peptide. Overall, our study reveals that short tethers offer the basis of an approach that facilitates measurement of adhesive interactions with single molecules presented at surfaces.

We report the synthesis of a mesogen that contains two nitrile groups (4-pentyl-3′,4′-dicyanobiphenyl, DCB), and the use of the mesogen in an investigation of the effects of multivalent ligand interactions on the ordering of liquid-crystalline phases at surfaces decorated with copper (Cu2+) ions. Differential scanning calorimetry (DSC) confirmed that DCB was miscible with nematic phases of 4-pentyl-4′-cyanobiphenyl (5CB). Quantitative measurement of the optical retardance of mixtures of DCB and 5CB in contact with surfaces decorated with Cu2+ (characterized by X-ray photoelectron spectroscopy, XPS) revealed a continuous ordering transition in the nematic LC as a function of increasing concentration of DCB (0.9−2 wt %). In contrast, Fourier transform infrared (FTIR) spectroscopy of 5 mM Cu2+ dissolved in bulk benzonitrile revealed no evidence of a change in nitrile coordination around the Cu2+ upon addition of 5CB or DCB, thus leading to the proposition that the effect of DCB on the ordering of the LC phases at Cu2+ decorated surfaces is due to divalent coordination interactions of DCB with the immobilized Cu2+ ions. This hypothesis was further tested by measurements of FTIR spectra and surface-induced ordering transitions of LC phases of DCB/5CB upon introduction of dimethylmethylphosphonate (DMMP), an organophosphonate that binds competitively with nitrile groups for Cu2+. These results, when combined, lead us to conclude that it is possible to substantially tune surface-induced ordering of LCs by manipulating the valency of the mesogens and thus coordination interactions of the LCs with metal ions immobilized on surfaces. Overall, the results of this study guide the design of multifunctional liquid crystals for use as chemoresponsive materials.