In this report, the metal-vapor synthesis (MVS) was used for the preparation of copper nanoparticles which was then used for the preparation of chitosan–copper nanocomposite. The antifungal activity of Cu@Chit NCs against two sclerotium-forming plant pathogenic fungi Sclerotium rolfsii (S. rolfsii) and Rhizoctonia solani (R. solani) AG-4 was evaluated in vitro and their effects on hyphal morphology, and sclerotia formation were observed for the first time. The NCs were prepared through impregnation of chitosan with colloid solution of copper nanoparticles in organic solvent (acetone or toluene). Transmission electron microscopy shows that the particles have predominantly spherical form, polydisperse character, the mean diameter about 2–3 nm and a rather uniform distribution in the chitosan matrice. Analysis of the small angle scattering curves suggests that the copper particles in the NCs with the size of ≤2 nm are mostly located in the chitosan pores with the same size. The effect of Cu@Chit NCs on fungal growth reveals some significant inhibitory activity against two tested fungi. The highest level of inhibition against S. rolfsii and R. solani AG-4 was observed using the high concentrations of Cu@Chit NC prepared using acetone as a solvent. A loss of the cytoplasm content, cytoplasmic coagulation, irregular shape of mycelia, or destruction in the hyphae was confirmed. The experiments demonstrate that the Cu@Chit NC synthesized via MVS using acetone was more effective than that of toluene in inhibiting fungal hyphae growth against R. solani AG-4 and S. rolfsii. The results show that the Cu@Chit NCs are fungicidal against both the tested fungus at high concentrations and the fungicidal or fungistatic activity is dependent on the tested fungus species.

Influenza A virus matrix protein M1 is one of the most important and abundant proteins in the virus particles broadly involved in essential processes of the viral life cycle. The absence of high-resolution data on the full-length M1 makes the structural investigation of the intact protein particularly important. We employed synchrotron small-angle X-ray scattering (SAXS), analytical ultracentrifugation and atomic force microscopy (AFM) to study the structure of M1 at acidic pH. The low-resolution structural models built from the SAXS data reveal a structurally anisotropic M1 molecule consisting of a compact NM-fragment and an extended and partially flexible C-terminal domain. The M1 monomers co-exist in solution with a small fraction of large clusters that have a layered architecture similar to that observed in the authentic influenza virions. AFM analysis on a lipid-like negatively charged surface reveals that M1 forms ordered stripes correlating well with the clusters observed by SAXS. The free NM-domain is monomeric in acidic solution with the overall structure similar to that observed in previously determined crystal structures. The NM-domain does not spontaneously self assemble supporting the key role of the C-terminus of M1 in the formation of supramolecular structures. Our results suggest that the flexibility of the C-terminus is an essential feature, which may be responsible for the multi-functionality of the entire protein. In particular, this flexibility could allow M1 to structurally organise the viral membrane to maintain the integrity and the shape of the intact influenza virus.