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Amphiphilic methacrylate copolymers (Si-co-EF) containing polysiloxane (Si) and mixed poly(oxyethylene)-perfluorohexyl (EF) side chains were synthesized with different compositions and used together with polysiloxane-functionalized nanoparticles as additives of condensation cured nanocomposite poly(siloxane) films. The mechanical properties of the nanocomposite films were consistent with the elastomeric behavior of the poly(siloxane) matrix without significant detriment from either the copolymer or the nanoparticles. Films were found to be markedly hydrophobic and liphophobic, with both properties being maximized at an intermediate content of EF units. The high enrichment in fluorine at the film surface was proven by angle-resolved X-ray photoelectron spectroscopy (AR-XPS). Long-term marine antifouling performance was evaluated in field immersion trials of test panels for up to 10 months of immersion. Both nanoparticles and amphiphilic copolymer were found to be highly effective in reducing the colonization of foulants, especially hard macrofoulants, when compared with control panels. Lowest percentage of surface coverage was 20% after 10 months of immersion (films with 4 wt% copolymer and 0.5 wt% nanoparticles), which was further decreased to less than 10% after exposure to a water jet for 10 s. The enhanced antifouling properties of coatings containing both nanoparticles and copolymer were confirmed by laboratory assays against the polychaete Ficopomatus enigmaticus and the diatom Navicula salinicola.

Here, we demonstrate that introduction of halogen atoms at the tyrosine 10 phenol ring of the DSGYEV sequence derived from the flexible amyloid-β N -terminus, promotes its self-assembly in the solid state. In particular, we report the crystal structures of two halogen-modified sequences, which we found to be stabilized in the solid state by halogen-mediated interactions. The structural study is corroborated by Non-Covalent Interaction (NCI) analysis. Our results prove that selective halogenation of an amino acid enhances the supramolecular organization of otherwise unstructured biologically-relevant sequences. This method may develop as a general strategy for stabilizing highly polymorphic peptide regions., Competing Interests: The authors declare no conflict of interest., (© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.)

Halogen bonding (XB) has been shown to be a powerful tool for promoting molecular self-assembly in different fields. The use of XB for noncovalent assembly of inorganic nanoparticles (NP) is, instead, quite limited, considering how extensively other interactions (i.e., electrostatic forces, hydrophobic effect, hydrogen bonding, etc.) have been exploited to modulate and program NP self-assembly. Here, we designed and synthesized XB-capable organic ligands that were efficiently used to functionalize the surface of gold NPs (AuNPs). XB-assisted AuNP self-assembly was attained in solution mixing AuNPs bearing XB-donor ligands with ditopic XB-acceptor molecules and AuNPs functionalized with XB-acceptor moieties. Likewise, a preliminary study of XB-driven adsorption of these AuNPs on surface was performed via Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D), used as an in situ tool for measuring mass changes upon XB-driven self-assembly.

Although intensively studied, the high-resolution crystal structure of the peptide DFNKF, the core-segment of human calcitonin, has never been described. Here we report how the use of iodination as a strategy to promote crystallisation and facilitate phase determination, allowed us to solve, for the first time, the single-crystal X-ray structure of a DFNKF derivative. Computational studies suggest that both the iodinated and the wild-type peptides populate very similar conformations. Furthermore, the conformer found in the solid-state structure is one of the most populated in solution, making the crystal structure a reliable model for the peptide in solution. The crystal structure of DFNKF(I) confirms the overall features of the amyloid cross-β spine and highlights how aromatic-aromatic interactions are important structural factors in the self-assembly of this peptide. A detailed analysis of such interactions is reported., (© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Dispersing hydrophobin HFBII under air saturated with perfluorohexane gas limits HFBII aggregation to nanometer-sizes. Critical basic findings include an unusual co-adsorption effect caused by the fluorocarbon gas, a strong acceleration of HFBII adsorption at the air/water interface, the incorporation of perfluorohexane into the interfacial film, the suppression of the fluid-to-solid 2D phase transition exhibited by HFBII monolayers under air, and a drastic change in film elasticity of both Gibbs and Langmuir films. As a result, perfluorohexane allows the formation of homogenous populations of spherical, narrowly dispersed, exceptionally stable, and echogenic microbubbles., (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Hydrophobins are natural surfactant proteins endowed with exceptional surface activity and film-forming capabilities and their use as effective "fluorine-free fluorosurfactants" has been recently reported. In order to increase their fluorophilicity further, here we report the preparation of a unique fluorous-modified hydrophobin, named F-HFBI. F-HFBI was found to be more effective than its wild-type parent protein HFBI at reducing interface tension of water at both air/water and oil/water interfaces, being particularly effective at the fluorous/water interface. F-HFBI was also found to largely retain the exceptionally good capability of forming strong and elastic films, typical of the hydrophobin family. Further studies by interface shear rheology and isothermal compression, alongside Quartz Crystal Microbalance and Atomic Force Microscopy, demonstrated the tendency of F-HFBI to form thicker films compared to the wild-type protein. These results suggest that F-HFBI may function as an effective compatibilizer for biphasic systems comprising a fluorous phase., (Copyright © 2015 The Authors. Published by Elsevier Inc. All rights reserved.)

(19)F-MRI offers unique opportunities to image diseases and track cells and therapeutic agents in vivo. Herein we report a superfluorinated molecular probe, herein called PERFECTA, possessing excellent cellular compatibility, and whose spectral properties, relaxation times, and sensitivity are promising for in vivo (19)F-MRI applications. The molecule, which bears 36 equivalent (19)F atoms and shows a single intense resonance peak, is easily synthesized via a simple one-step reaction and is formulated in water with high stability using trivial reagents and methods.