| Summary: | Cage-like proteins such as E2 from Bacillus stearothermophilus, ferritins and heat shock proteins have surfaces which can be modified to generate nanomaterials with multiple functionalities. Limited studies have been carried out on E2 and its characteristics in terms of metal loading. In this work, E2 wild type protein (E2-WT) and its mutants namely the LE6, where the loop is replaced with six glutamic acids, and LFer, in which it is designed to mimic the key amino acids groups in frog M-ferritin catalytic center, were investigated to determine its characteristics by measuring the hydrodynamic size of the cage using Dynamic Light Scattering (DLS) and the structure using Transmission Electron Microscope (TEM) after loading with metals such as iron, manganese and cadmium. It was found that the loading of iron and manganese to the engineered mutant E2 proteins did not affect the hydrodynamic size and the structure of the protein cage thus proving its stability in the synthesis of nanoparticles. However, the loading of cadmium in this work has shown an increase in its hydrodynamic size by at least 1000 nm caused by the cadmium sulphide salt that was used for loading.
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