An octameric trans-membrane channel protein, MspA, has been successfully isolated from Mycobacterial smegmatis and purified to obtain crystals. A full analytical assessment has been carried out to authenticate the protein structure, including gel electrophoresis, spectroscopy (fluorescence, UV, FTIR, NMR), HPLC, Bradford protein assay, and dynamic light scattering. An X-ray crystallographic study is underway. Channel activity of pure and chemically modified MspA has been investigated to reveal a significant current conductance. Ru(II) complexes show significant gating with purified MspA. This phenomenon has future potential in DNA sequencing and development of antimycobacterial drugs (channel blockers). A Ru(II)-phenanthroline-bipyridinium-maleimide complex has been synthesized and reacted with the thiol group of cystein, located in the periplasmatic loop of a mutant of MspA (A96C). Photoelectrical properties of this protein-metal complex have been investigated and show a significant current conductance. This unique ability of the protein has potential application as the first ever 'protein nano solar cell'.

Purification and analytical assessment of the mycobacterial porin MspA and investigation of its channel activity and potential use for a protein nano-solar cell

242nd National Meeting (2011)

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