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Overexpression, purification, and pharmacological activity of a biosynthetically derived conopeptide

Kumar, Ganesan Senthil and Ramasamy, Palanisamy and Sikdar, Sujit K and Sarma, Siddhartha P (2005) Overexpression, purification, and pharmacological activity of a biosynthetically derived conopeptide. In: Biochemical and Biophysical Research Communications, 335 (3). pp. 965-972.


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A high yielding fusion protein system based on the protein cytochrome $b_{5}$ 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 4 mg of purified peptide from a 500 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 $^{15}N/^{13}C$-enriched conopeptide.

Item Type: Journal Article
Publication: Biochemical and Biophysical Research Communications
Publisher: Elsevier Inc
Additional Information: Copyright for this article belongs to Elsevier Inc.
Keywords: Mo1659;Conus monile;Conotoxin;Isotopic 15N/13C labeling of peptides;cytb5 fusion;Potassium channels;Heteronuclear NMR
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 23 Nov 2007
Last Modified: 19 Sep 2010 04:20
URI: http://eprints.iisc.ac.in/id/eprint/3809

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