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

Abstract：

: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 4mg of purified peptide from a 500ml 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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kumar GS,Ramasamy P,Sikdar SK,Sarma SP

doi

10.1016/j.bbrc.2005.08.002

subject

Has Abstract

pub_date

2005-09-30 00:00:00

pages

965-72

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01677-3

journal_volume

335

pub_type

杂志文章

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