Although thermoplastic materials are mostly derived from petro-chemicals, it would be highly desirable, from a sustainability perspective, to produce them instead from renewable biopolymers. Unfortunately, biopolymers exhibiting thermoplastic behaviour and which preserve their mechanical properties post processing are essentially non-existent. The robust sucker ring teeth (SRT) from squid and cuttlefish are one notable exception of thermoplastic biopolymers. Here we describe thermoplastic processing of squid SRT via hot extrusion of fibres, demonstrating the potential suitability of these materials for large-scale thermal forming. Using high-resolution in situ X-ray diffraction and vibrational spectroscopy, we elucidate the molecular and nanoscale features responsible for this behaviour and show that SRT consist of semi-crystalline polymers, whereby heat-resistant, nanocrystalline β-sheets embedded within an amorphous matrix are organized into a hexagonally packed nanofibrillar lattice. This study provides key insights for the molecular design of biomimetic protein- and peptide-based thermoplastic structural biopolymers with potential biomedical and 3D printing applications.

Selective interactions of ions with charge-neutral saccharides can have far-reaching consequences in biological and wet-technological contexts but have so far been observed only indirectly. Here, we directly quantify by total-reflection X-ray fluorescence the preferential accumulation of ions near uncharged saccharide surfaces in the form of glycolipid Langmuir monolayers at air/water interfaces exhibiting different levels of structural ordering. Selective interactions with ions from the aqueous subphase are observed for monolayers featuring crystalline ordering of the saccharide headgroups, as determined by grazing-incidence X-ray diffraction. The attracted ion species depend on the structural motifs displayed by the ordered saccharide layer. Our results may constitute a basis to understand the salt-specific swelling of wood materials and various phenomena in membrane biophysics.

The outer surfaces of Gram-negative bacteria are composed of lipopolysaccharide (LPS) molecules exposing oligo- and polysaccharides to the aqueous environment. This unique, structurally complex biological interface is of great scientific interest as it mediates the interaction of bacteria with antimicrobial agents as well as with neighboring bacteria in colonies and biofilms. Structural studies on LPS surfaces, however, have so far dealt almost exclusively with rough mutant LPS of reduced molecular complexity and limited biological relevance. Here, by using neutron reflectometry, we structurally characterize planar monolayers of wild-type LPS from Escherichia coli O55:B5 featuring strain-specific O-side chains in the presence and absence of divalent cations and under controlled interaction conditions. The model used for the reflectivity analysis is self-consistent and based on the volume fraction profiles of all chemical components. The saccharide profiles are found to be bimodal, with dense inner oligosaccharides and more dilute, extended O-side chains. For interacting LPS monolayers, we establish the pressure-distance curve and determine the distance-dependent saccharide conformation.

Membrane-bound oligosaccharides with specific chemistries are known to promote tight adhesion between adjacent membranes via the formation of weak saccharide bonds. However, in the literature, one can find scattered evidence that other, more abundant saccharide chemistries exhibit similar behavior. Here, the influence of various glycolipids on the interaction between adjacent membranes is systematically investigated with the help of small-and wide-angle x-ray scattering and complementary neutron diffraction experiments. Added electrostatic repulsion between the membrane surfaces is used to identify the formation of saccharide bonds and to challenge their stability against tensile stress. Some of the saccharide headgroup types investigated are able to bind adjacent membranes together, but this ability has no significant influence on the membrane bending rigidity. Our results indicate that glycolipid-mediated membrane adhesion is a highly abundant phenomenon and therefore potentially of great biological relevance.

Poly(ethylene glycol) (PEG) brushes are reputed for their ability to prevent undesired protein adsorption to material surfaces exposed to biological fluids. Here, protein adsorption out of human blood serum onto PEG brushes anchored to solid-supported lipid monolayers was characterized by neutron reflectometry, yielding volume fraction profiles of lipid headgroups, PEG, and adsorbed proteins at subnanometer resolution. For both PEGylated and non-PEGylated lipid surfaces, serum proteins adsorb as a thin layer of approximately 10 Å, overlapping with the headgroup region. This layer corresponds to primary adsorption at the grafting surface and resists rinsing. A second diffuse protein layer overlaps with the periphery of the PEG brush and is attributed to ternary adsorption due to protein-PEG attraction. This second layer disappears upon rinsing, thus providing a first observation of the structural effect of rinsing on protein adsorption to PEG brushes.