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Expression and characterization of recombinant kurtoxin, an inhibitor of T-type voltage-gated calcium channels.

Abstract：

:Kurtoxin, a 63-amino acid peptide stabilized by four disulfide bonds, is the first reported peptide inhibitor of T-type voltage-gated calcium channels. Although T-type calcium channels have been implicated in a number of disease states, including epilepsy, chronic pain, hypertension and cancer, the lack of selective inhibitors has slowed progress in understanding their precise roles. Kurtoxin is a potentially valuable tool with which to study T-type calcium channels. However, because of the limited availability of the native protein, little is known about the structure and molecular mechanism of kurtoxin. Here we report the expression of kurtoxin in Escherichia coli and the structural and functional characterization of the recombinant protein. The disulfide bond pairings and secondary structure of recombinant kurtoxin were characterized through enzymatic cleavage, mass analysis and CD spectroscopy. Recombinant kurtoxin almost completely inhibited the T-type calcium channel in a manner identical to the native toxin. The availability of recombinant kurtoxin that is identical to the native toxin should help in the study of T-type calcium channels and enable development of new strategies for producing even more-selective T-type calcium channel inhibitors and for investigating the molecular basis of the toxin-channel interactions.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lee CW,Eu YJ,Min HJ,Cho EM,Lee JH,Kim HH,Nah SY,Swartz KJ,Kim JI

doi

10.1016/j.bbrc.2011.11.003

subject

Has Abstract

pub_date

2011-12-16 00:00:00

pages

277-82

issue

3-4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)02002-X

journal_volume

416

pub_type

杂志文章

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