Synthesis and Characterization of Durable Antibiofilm and Antiviral Silane-Phosphonium Thin Coatings for Medical and Agricultural Applications.

Pathogens such as bacteria and viruses cause disease in a range of hosts, from humans to plants. Bacterial biofilms, communities of bacteria, e.g., Staphylococcus aureusand Escherichia coli, attached to the surface, create a protective layer that enhances their survival in harsh environments and resistance to antibiotics and the host's immune system. Biofilms are commonly associated with food spoilage and chronic infections, posing challenges for treatment and prevention. Tomato brown rugose fruit virus (ToBRFV), a newly discovered tobamovirus, infects tomato plants, causing unique symptoms on the fruit, posing a risk for tomato production. The present study focuses on the effectiveness of silane-phosphonium thin coatings on polymeric films, e.g., polypropylene. Phosphonium has significant antibacterial activity and is less susceptible to antibacterial resistance, making it a safer alternative with a reduced environmental impact. We successfully synthesized silane-phosphonium monomers as confirmed by 31P NMR and mass spectrometry. The chemical composition, thickness, morphology, and wetting properties of the coatings were tested by Fourier-transform infrared spectroscopy with attenuated total reflectance, focused ion beam, atomic force microscopy, environmental scanning electron microscope, and contact angle (CA) measurements. The antibiofilm and antibacterial activities of the coatings were tested against S. aureus and E. coli, while the antiviral activity was evaluated against ToBRFV. The significant antibiofilm and antiviral activity suggests applications in various fields including medicine, agriculture, and the food industry.

Ctr1 Intracellular Loop Is Involved in the Copper Transfer Mechanism to the Atox1 Metallochaperone.

Understanding the human copper cycle is essential to understand the role of metals in promoting neurological diseases and disorders. One of the cycles controlling the cellular concentration and distribution of copper involves the copper transporter, Ctr1; the metallochaperone, Atox1; and the ATP7B transporter. It has been shown that the C-terminus of Ctr1, specifically the last three amino acids, HCH, is involved in both copper coordination and the transfer mechanism to Atox1. In contrast, the role of the intracellular loop of Ctr1, which is an additional intracellular segment of Ctr1, in facilitating the copper transfer mechanism has not been investigated yet. Here, we combine various biophysical methods to explore the interaction between this Ctr1 segment and metallochaperone Atox1 and clearly demonstrate that the Ctr1 intracellular loop (1) can coordinate Cu(I) via interactions with the side chains of one histidine and two methionine residues and (2) closely interacts with the Atox1 metallochaperone. Our findings are another important step in elucidating the mechanistic details of the eukaryotic copper cycle.