Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10768785 | Biochemical and Biophysical Research Communications | 2005 | 8 Pages |
Abstract
A high yielding fusion protein system based on the protein cytochrome b5 has been used for the production of novel 13-residue acyclic conopeptide. This peptide, Mo1659, can be liberated from the carrier protein using CNBr cleavage and subsequent purification using RP-HPLC methods. The yield of isotopically enriched peptides is high, ranging from 3 to 4Â mg of purified peptide from a 500Â ml culture, indicating that this system can be widely used for peptide production. Biosynthetic Mo1659 is active on non-inactivating K+ channel much like the natural Mo1659, despite the absence of C-terminal amidation. Heteronuclear NMR studies show that the peptide exists in a conformational equilibrium involving proline-10. To our knowledge this is the first report of the production of an isotopically 15N/13C-enriched conopeptide.
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Authors
Ganesan Senthil Kumar, Palanisamy Ramasamy, Sujit K. Sikdar, Siddhartha P. Sarma,