ORGN 877 |
| Proteins can be tailored to serve specific needs by site-directed mutagenesis. However, their use in nanotechnology has been severely hampered by the problem that most proteins lose their structural integrity in a non-native environment, impeding their use in any technical processes. The MspA porin from M. smegmatis is an extremely stable protein, retaining its channel structure even after boiling in 3% SDS or extraction with organic solvents. MspA features a very hydrophobic “docking region” at the stem of its “goblet”, whereas its “rim” section is formed by alternating hydrophilic and hydrophobic residues so that it is much more hydrophilic. The geometric dimensions of the “docking region” (length = 3.7 nm, diameter = 4.9 nm) are suitable for its reconstitution in various cell membranes. Because of its extraordinary stability, MspA has great prospects for future use in analytical, biochemical and medicinal applications. Emerging applications involving a bio-nanotechnology application on surfaces and a sensing device for antibiotics against tuberculosis will be presented.
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Proteins, Peptides, Amino Acids, and Enzyme Inhibitors
8:00 AM-12:00 PM, Thursday, 14 September 2006 Moscone Center -- Room 131, Oral
Division of Organic Chemistry |
