ABSTRACT
This work aims to synthesize, characterize and evaluate the biological activity of nanochitosan (NQ) prepared from shrimp, showing an innovative character and correlating with sustainable development, in promoting an alternative to the solid waste (shrimp) shell and a biological application of the novel nanomaterial. The NQ synthesis was carried out by the alkaline deacetylation process of chitin obtained of the demineralization, deproteinization and deodorization steps from shrimp shells. NQ was characterized by X-ray Powder Diffraction (XRD), Fourier Transform infrared spectroscopy (FTIR), Scanning electron microscopy with energy dispersive X-ray spectroscopy (SEM-EDS), N2 porosimetry (BET/BJH methods), zeta potential (ZP) and zero charge point (pHZCP). To evaluate the safety profile was carried out the cytotoxicity, DCFHA and NO tests in 293T and HaCat cell lines. Regarding the cell viability, NQ did not show toxicity for the tested cell lines. In the evaluation of the ROS production and NO tests, there was no increase in the levels of free radicals and between the negative control, respectively. Therefore, NQ does not present cytotoxicity in the cell lines tested (10, 30, 100 and 300 µg mL-1), proposing new perspectives on the use of NQ as a potential nanomaterial for biomedical applications.
Subject(s)
Chitosan , Decapoda , Nanostructures , Chitosan/chemistry , Chitosan/toxicity , Nanostructures/chemistry , Nanostructures/toxicity , Reactive Oxygen Species/metabolism , Decapoda/chemistry , Humans , HEK293 Cells , Keratinocytes/metabolism , Cell Survival/drug effects , Nitrites/metabolism , Nitrates/metabolismABSTRACT
The objectives of this study were to evaluate tetrahydropyridine derivatives as efflux inhibitors and to understand the mechanism of action of the compounds by in silico studies. Minimum inhibitory concentration (MIC) determination, fluorometric methods and docking simulations were performed. The compounds NUNL02, NUNL09 and NUNL10 inhibited efflux, and NUNL02 is very likely a substrate of the transporter protein AcrB. Docking studies suggested that the mechanism of action could be by competition with substrate for binding sites and protein residues. We showed for the first time the potential of tetrahydropyridines as efflux inhibitors and highlighted compound NUNL02 as an AcrB-specific inhibitor. Docking studies suggested that competition is the putative mechanism of action of these compounds.
