Recombinant expression and downstream processing of the disulfide-rich tumor-targeting peptide chlorotoxin.

ABSTRACT: Chlorotoxin (CTX) is a scorpion-derived disulfide-rich peptide that targets malignant tumors by binding the cell surface matrix metalloproteinase-2 and annexin A2. Various CTXs labeled with functional moieties have shown great potential for tumor diagnosis and treatment. In the present study, we established an efficient approach for preparing mature CTX that may be used for experimental and therapeutic purposes. The designed CTX precursors carried either a 6xHis-tag or a 6xHis-tag and a glutathione transferase (GST)-tag and were recombinantly expressed in Escherichia coli. Following S-sulfonation, the precursors were purified using immobilized metal-ion affinity chromatography. Subsequent to the removal of the tag by enterokinase cleavage and in vitro oxidative refolding, mat

SUBMITTER: Wang XM 

PROVIDER: S-EPMC3797302 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature