Description:
<jats:p xml:lang="en">
Chlorotoxin (CLTX) is a neurotoxin found in the venom of
the Israeli scorpion, Leirius
quinquestriatus. It contains 36-amino acids with four disulfide bonds and inhibits
low-conductance chloride channels. CLTX also binds to matrix
metalloproteinase-2 (MMP-2) selectively. The synthesis of chlorotoxin using
solid phase peptide synthesis (SPPS) is very difficult and has a very low yield
(&lt;1%) due to high number of amino acid sequence. In this work, to improve the
efficiency of the synthesis, native chemical ligation was applied. In this strategy,
chlorotoxin sequence was split into two parts having 15 and 21 amino acids. 21-mer
peptide was synthesized in its native form based on
9-fluorenylmethyloxycarbonyl (Fmoc) chemistry. 15-mer peptide was synthesized
having o-aminoanilide linker on C-terminal. These parts were coupled by native
chemical ligation to produce chlorotoxin. </jats:p>