An aqueous chemical reaction has been used to prepare antifungal ZnS: Mn nanostructures, from manganese chloride, zinc acetate and thioacetamide in aqueous solution. The nanoparticle size has been controlled using thioglycolic acid as a capping factor. The major feature of the ZnS:Mn nanoparticles of average diameter ~ 2.73 nm is that possible preparing the sample from sources non-toxic precursors. The manufactured ZnS:Mn nanoparticles were identified and characterized to investigate the structure, morphology, composition of components of the nanoparticles and optical properties using (XRD, SEM, EDS and UV-Vis spectroscopy) techniques respectively. The agar dilution mechanism used to evaluate of the antifungal activity using ZnS:Mn nanopart

The azo ligand obtained from the diazotization reaction of 2-aminobenzothiazole and 4- nitroaniline yielded a novel series of complexes with Co(II), Ni(II), Cu(II), and Zn(II) ions. The complexes were investigated using spectral techniques such as UV-Vis, FT-IR, 1H and 13C NMR spectroscopic analyses, LC-MS and atomic absorption spectrometry, electrical conductivity, and magnetic susceptibility. The molar ratio of the synthesized compounds was determined using the ligand exchange ratio, which revealed the metal-ligand ratios in the isolated complexes were 1:2. The synthesized complexes were tested for antimicrobial activity against S. aureus, E. coli, C. albicans, and C. tropicalis bacterial species. Additionally, their binding affinities we

Flexible molecular docking is a computational method of structure-based drug design to evaluate binding interactions between receptor and ligand and identify the ligand conformation within the receptor pocket. Currently, various molecular docking programs are extensively applied; therefore, realizing accuracy and performance of the various docking programs could have a significant value. In this comparative study, the performance and accuracy of three widely used non-commercial docking software (AutoDock Vina, 1-Click Docking, and UCSF DOCK) was evaluated through investigations of the predicted binding affinity and binding conformation of the same set of small molecules (HIV-1 protease inhibitors) and a protein target HIV-1 protease enzy