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Designing a surface that can disinfect itself can reduce labor-intensive cleanings and harmful waste, and mitigate spread of surface borne diseases. Additionally, since COVID-19 is an airborne pathogen, surface modification of masks and filters could assist with infection control. Styrene-maleic acid (SMA) copolymers and their derivatives were shown to have lipid-bilayer disrupting properties, making them candidates as anti-viral materials. A series of network polymers with styrene-maleic acid-based polymers and control over polymer chain-length and composition were synthesized. All the polymers formed mechanically robust structures, with tunable Young's moduli on the order of MPa, and tunable swelling capability in water. The SMA-based bulk materials, containing a zwitterionic polar unit, showed excellent lipid disrupting properties, being up to 2 times more efficient than a 10% Triton solution. The highest performance was observed for materials with lower crosslink densities or shorter chain-lengths, with lipid disruption capability correlating with swelling ratio. Additionally, the material can capture the spike protein of SARS-CoV-2, with up to 90% efficiency. Both the lipid disrupting and spike protein capture ability could be repeated for multiple cycles. Finally, the materials are shown to modify various porous and non-porous substrates including surgical and KN95 masks. Functional network modified masks had up to 6 times higher bilayer disruption ability than the unmodified masks without inhibiting airflow. 

Coronavirus disease 2019 (COVID‐19) has significantly impacted human health, the global economy, and society. Viruses residing on common surfaces represent a potential source of contamination for the general population. Spike binding peptide 1, SBP1 is a 23 amino acid peptide, which has micromolar binding affinity (1.3 μM) towards the spike protein receptor‐binding domain. We hypothesize that if we can covalently immobilize this SBP1 peptide in a covalent crosslinked network system, we can develop a surface that would preferentially bind spike protein and, therefore, which could limit viral spread. A series of covalently crosslinked networks of hydroxy ethyl acrylate (HEA) with different primary chain lengths and crosslinker density was prepared. Later, this network system was functionalized using 2% SBP1 peptide. Our study found that with a shorter chain length and lower crosslinker density, the HEA network system alone could capture almost 80% of the spike protein. We reported that the efficiency could be enhanced almost by 17% with higher crosslinker density.

 

For more than 40 years, protein–polymer conjugates have been widely used for many applications, industrially and biomedically. These bioconjugates have been shown to modulate the activity and stability of various proteins while introducing reusability and new activities that can be used for drug delivery, and to improve pharmacokinetic ability and stimuli-responsiveness. Techniques such as RDRP, ROMP and “click” have routinely been utilized for the development of well-defined bioconjugate and polymeric materials. The synthesis of bioconjugate materials often takes advantage of the natural amino acids present within the protein and peptide structures for a host of coupling chemistries. Polymer modification may elicit increased or decreased activity, activity retention under harsh conditions, and prolonged activity in vivo and in vitro , and introduce stimuli responsiveness. Bioconjugation has resulted in modulated thermal stability, chemical stability, storage stability, half-life and reusability. In this review we aim to provide a brief account of the field, highlight a wide range of behaviors caused by polymer conjugation, and provide directions for future work. 

Protein‐polymer bioconjugates present a way to make enzymes more efficient and robust for industrial and medicinal applications. While much work has focused on mono‐functional conjugates, that is, conjugates with one type of polymer attached such as poly(ethylene glycol) or poly(N‐isopropylacrylamide), there is a practical interest in gaining additional functionality by synthesizing well‐defined bifunctional conjugates in a hetero‐arm star copolymer architecture with protein as the core. Using ubiquitin as a model protein, a synthetic scheme is developed to attach two different polymers (oligo(ethylene oxide) methacrylate and N,N‐dimethylacrylamide) directly to the protein surface, using orthogonal conjugation chemistries and grafting‐from by photochemical living radical polymerization techniques. The additional complexity arising from attempts to selectively modify multiple sites led to decreased polymerization performance and indicates that initiators for continuous activator regeneration atom transfer radical polymerization and reversible addition‐fragmentation chain transfer polymerization are not well‐suited to bifunctional bioconjugates applications under the studied conditions. Nonetheless, the polymerization conditions preserve the native fold of the ubiquitin and enable production of a hetero‐arm star protein‐polymer bioconjugate.

 

The ubiquitin ligase CHIP catalyzes covalent attachment of ubiquitin to unfolded proteins chaperoned by the heat shock proteins Hsp70/Hsc70 and Hsp90. CHIP interacts with Hsp70/Hsc70 and Hsp90 by binding of a C-terminal IEEVD motif found in Hsp70/Hsc70 and Hsp90 to the tetratricopeptide repeat (TPR) domain of CHIP. Although recruitment of heat shock proteins to CHIP via interaction with the CHIP-TPR domain is well established, alterations in structure and dynamics of CHIP upon binding are not well understood. In particular, the absence of a structure for CHIP-TPR in the free form presents a significant limitation upon studies seeking to rationally design inhibitors that may disrupt interactions between CHIP and heat shock proteins. Here we report the 1H, 13C, and 15N backbone and side chain chemical shift assignments for CHIP-TPR in the free form, and backbone chemical shift assignments for CHIP-TPR in the IEEVD-bound form. The NMR resonance assignments will enable further studies examining the roles of dynamics and structure in regulating interactions between CHIP and the heat shock proteins Hsp70/Hsc70 and Hsp90.