Self-healing polymer-based coatings have emerged as a new generation of adaptive protective materials capable of restoring their structure and function after damage. This review provides a comprehensive analysis of current strategies enabling autonomous or externally triggered repair in polymeric films, including encapsulation, reversible chemistry, and microvascular network formation. Emphasis is placed on polymer–inorganic hybrid composites and vitrimeric systems, which integrate barrier protection with stimuli-responsive healing and recyclability. Comparative performance across different matrices—epoxy, polyurethane, silicone, and polyimine—is discussed in relation to corrosion protection and biomedical interfaces. The review also highlights how dynamic covalent and supramolecular interactions in hydrogels enable self-repair under physiological conditions. Recent advances demonstrate that tailoring interfacial compatibility, healing kinetics, and trigger specificity can achieve repeatable, multi-cycle recovery of both mechanical integrity and functional performance. A representative selection of published patents is also shown to illustrate recent technological advancements in the field. Finally, key challenges are identified in standardizing evaluation protocols, ensuring long-term stability, and scaling sustainable manufacturing. Collectively, these developments illustrate the growing maturity of self-healing polymer coatings as multifunctional materials bridging engineering, environmental, and biomedical applications.

Control over the placement and activity of biomolecules on solid surfaces is a key challenge in bionanotechnology. While covalent approaches excel in performance, physical attachment approaches excel in ease of processing, which is equally important in many applications. We show how the precision of recombinant protein engineering can be harnessed to design and produce protein-based diblock polymers with a silica-binding and highly hydrophilic elastin-like domain that self-assembles on silica surfaces and nanoparticles to form stable polypeptide brushes that can be used as a scaffold for later biofunctionalization. From atomic force microscopy-based single-molecule force spectroscopy, we find that individual silica-binding peptides have high unbinding rates. Nevertheless, from quartz crystal microbalance measurements, we find that the self-assembled polypeptide brushes cannot easily be rinsed off. From atomic force microscopy imaging and bulk dynamic light scattering, we find that the binding to silica induces fibrillar self-assembly of the peptides. Hence, we conclude that the unexpected stability of these self-assembled polypeptide brushes is at least in part due to peptide–peptide interactions of the silica-binding blocks at the silica surface.

In the quest for advancing the performance of metallic implants, surface modification emerges as a pivotal strategy to mitigate ion depletion, enhance the host's biological response, and exhibit anti-microbial behavior with reduced cytotoxicity. In this study, we developed a non-traditional electrophoretic deposition (EPD) hybrid coating for medical-grade stainless steel 316 L (SS316L) surfaces covered with a segmented polyurethane (SPU). These coatings are composed of anatase TiO₂ nanotubes (TiO₂_A), and antibiotics (nisin N or gentamicin G). We characterized the modified metals using FTIR and Raman spectroscopy, contact angle measurements, AFM, TGA, SEM-EDX, as well as assessing their antimicrobial response and cell cytotoxicity. The results demonstrate the formation of porous surfaces with embedded nanotubes and antibiotics within and on the polyurethane surfaces. Samples with SPU+ TiO₂_AG EPD exhibited superior coverage, antimicrobial properties, and enhanced viability compared to cases where only particles or antibiotics were coated individually. Additionally, samples of SPU+ TiO₂_AN EPD displayed favorable hydrophilicity and suitable cytotoxicity. Therefore, the synergistic effect of nanoparticles and antibiotics positively influences the functionality of the coating.

Protein conformational changes are essential to biological function, and the heterogeneous nature of the corresponding protein states provokes an interest to measure conformational changes at the single molecule level.