Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Life Sci ; 234: 116758, 2019 Oct 01.
Article in English | MEDLINE | ID: mdl-31421083

ABSTRACT

In this work, fluorescent copper oxide nanoparticles (CuO NPs) were green synthesized using viable cells, cell lysate supernatant (CLS) and protein extracts of luminescent Vibrio sp. VLC. Biogenic CuO NPs were then characterized by XRD, FTIR, UV/Vis spectroscopy, TEM, DLS, and PL spectroscopy. Results showed that CLS method was more efficient for CuO NPs production, therefore CuO NPs synthesized by this method from copper sulfate (CuO NPs-1) and/or copper nitrate (CuO NPs-2) were used for further studies. The crystallite size of polydispersed CuO NPs-1 and CuO NPs-2 were about 8.83 and 8.77 nm, respectively indicating their suitability for biological applications. Antibacterial activity of CuO NPs was determined using broth microdilution, well diffusion agar, and time-kill curves methods. Both CuO NP-1 and CuO NP-2 inhibited bacterial growth at the minimum inhibitory concentration (MIC) of 625 mg/L except St. mutants (MIC = 1250 mg/L). Emission of fluorescent light from the surface of NPs was increased when exposed to Cd2+, As2+ and Hg2+ ions but decreased by Pb2+ ions. Results showed that CuO NP-1 had anticancer properties against KYSE30 esophageal cancer cell line (IC50 = 13.96 mg/L) while no higher cytotoxic effects were observed on Human Dermal Fibroblasts (HDF) (IC50 = 48.88 mg/L).


Subject(s)
Anti-Bacterial Agents/pharmacology , Antineoplastic Agents/pharmacology , Copper/pharmacology , Esophageal Neoplasms/drug therapy , Fluorescent Dyes/chemistry , Metals, Heavy/analysis , Nanoparticles/chemistry , Anti-Bacterial Agents/chemistry , Antineoplastic Agents/chemistry , Bacteria/drug effects , Bacterial Infections/drug therapy , Cell Line, Tumor , Copper/chemistry , Green Chemistry Technology/methods , Humans , Spectrometry, Fluorescence/methods , Vibrio/chemistry
2.
Int J Biol Macromol ; 106: 284-292, 2018 Jan.
Article in English | MEDLINE | ID: mdl-28782614

ABSTRACT

Salts exist in any cell and living organism in contact with biological macromolecules. How these salts affect biomolecules such as enzyme is important from both basic sciences and practical technologies. It was observed that divalent salts can change structure and function of protein at higher concentrations. Here, we investigated the effect of divalent salt on the behavior of a multimeric enzyme. We treated glucose oxidase as dimer-active enzyme in different CaCl2 concentration and seen that the enzyme become inactive at high concentration of salt. These experimental results are in agreement with recently published researches. To find a possible mechanism, a series of molecular dynamics simulation of the enzyme were performed at different salt concentration. According to the MD simulation, the conformational changes at the active site and FAD-binding site support the hypothesis of enzyme inactivation at high CaCl2 concentration. MD simulations also showed that enzyme has an unstable conformation at higher salt concentration which is in agreement with our experimental data. Detailed structural properties of the enzyme have been analyzed under different conditions. To the best of our knowledge, this is the first study that bears detailed structural mechanism about the salt effects on multimeric macromolecules.


Subject(s)
Calcium Chloride/chemistry , Flavin-Adenine Dinucleotide/chemistry , Glucose Oxidase/chemistry , Molecular Dynamics Simulation , Aspergillus niger/chemistry , Aspergillus niger/enzymology , Catalytic Domain , Enzyme Stability , Glucose Oxidase/isolation & purification , Protein Binding , Protein Conformation, alpha-Helical , Protein Conformation, beta-Strand , Protein Interaction Domains and Motifs , Protein Multimerization
SELECTION OF CITATIONS
SEARCH DETAIL
...