Ice-binding proteins (IBP) facilitate survival under extreme conditions in diverse life forms. IBPs in polar fishes block further growth of internalized environmental ice and inhibit ice recrystallization of accumulated internal crystals. Algae use IBPs to structure ice, while ice adhesion is critical for the Antarctic bacterium Marinomonas primoryensis. Successful translation of this natural cryoprotective ability into man-made materials holds great promise but is still in its infancy. This review covers recent advances in the field of ice-binding proteins and their synthetic analogues, highlighting fundamental insights into IBP functioning as a foundation for the knowledge-based development of cheap, bio-inspired mimics through scalable production routes. Recent advances in the utilisation of IBPs and their analogues to e.g. improve cryopreservation, ice-templating strategies, gas hydrate inhibition and other technologies are presented.

Significance: Controlling ice crystal growth is a grand scientific challenge with major technological ramifications. Some cold-adapted organisms such as fish and arthropods are protected against ice growth by producing antifreeze proteins (AFPs). These AFPs adsorb onto embryonic ice crystals, thereby inhibiting their growth. On a macroscopic level, this is evidenced by ice recrystallization inhibition (IRI) and thermal hysteresis (TH) activity. Our research demonstrates the absence of a clear correlation between TH and IRI activities, and underlines the importance of the extent of supercooling and annealing time on the efficacy of AFPs in blocking ice growth. We emphasize that successful application of AFPs and synthetic analogues in innovative strategies for cryoprotection, cryopreservation, and antiicing technologies requires optimization tailored toward the specific purpose.

Supramolecular block copolymers are becoming attractive materials in nascent optoelectronic and catalytic technologies. However, their dynamic nature precludes the straightforward tuning and analysis of the polymer’s structure. Here we report the elucidation on the microstructure of triarylamine triamide-based supramolecular block copolymers through a comprehensive battery of spectroscopic, theoretical, and super-resolution microscopic techniques. Via spectroscopic analysis we demonstrate that the direct mixing of preassembled homopolymers and the copolymerization induced by slow cooling of monomers lead to the formation of the same copolymer’s architecture. The small but pronounced deviation of the experimental spectra from the linear combination of the homopolymers’ spectra hints at the formation of block copolymers. A mass balance model is introduced to further unravel the microstructure of the copolymers formed, and it confirms that stable multiblock supramolecular copolymers can be accessed from different routes. The multiblock structure of the supramolecular copolymers originates from the fine balance between favorable hydrogen-bonding interactions and a small mismatch penalty between two different monomers. Finally, we visualized the formation of the supramolecular block copolymers by adapting a recently developed super-resolution microscopy technique, interface point accumulation for imaging in nanoscale topography (iPAINT), for visualizing the architectures formed in organic media. Combining multiple techniques was crucial to unveil the microstructure of these complex dynamic supramolecular systems.