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Bio-templates such as proteins, lipids offer rich structural and functional diversity for the synthesis of nanoparticles by controlling their shape, size and orientation. In this work we have exploited a pH dependent folding-refolding feature of Horse Spleen Apoferritin (HsAFr) to synthesize copper and manganese oxide nanoparticles in a controlled manner. Two methods of preparation were used in this study. In the first method, Copper Sulphate (100 mM) and Manganese Chloride (4.8 mM) have been incubated with the protein and the pH dynamically adjusted for homogeneous incorporation of the metal ions into the HsAFr shell. The second study involved the incorporation of Cu2+ and Mn2+ inside HsAFr cavity and subsequent designing of nanoclusters of the respective oxides. UV, fluorescence and far-UV circular dichroism (far-UV CD) spectroscopic techniques have been used to study the mineralization effect of the metal inside the HsAFr cavity. Size determination carried out using XRD suggested an average size ranging from 20-30 nm. The EPR of the nanoclusters show that incorporation of Mn2+ leads to a characteristic magnetoferritin behavior.

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This work presents the design of sub-micron-sized capsules of Cytochrome c (cyt c) in the range 300-350 nm and the conformational transitions of the protein that occur when the films of these capsules spread at the air/buffer interface are subjected to repeated compression-expansion cycles. Steady state fluorescence, time-resolved fluorescence, and circular dichroic (CD) spectra have been used to study the highly compact native conformation (70% helicity) of the protein in the capsules and its stability has been analyzed using cyclic voltammetry. The capsules have been characterized using zeta sizer and high resolution transmission electron microscopy (HRTEM). Surface concentration-surface pressure (Γ-π) isotherms of the films of the capsules spread at air/buffer interface following compression-expansion show destabilizing effect on cyt c. FTIR and CD spectra of these films skimmed from the surface show that the protein transitions gradually from its native helical to an anomalous beta sheet aggregated state. This results from a competition between stabilizing hydrated polar segments of the protein in the capsule and destabilizing nonspecific hydrophobic interactions arising at the air/buffer interface. This 2D model could further our understanding of the spatial and temporal roles of proteins in confined spaces and also in the design of new drug delivery vehicles using proteins.