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Bioassay driven purification of ButaIT
A structure model of ButaIT, generated from the Swiss-model protein modeling server based on the structural coordinates of chlorotoxin [ 38 ] and insectotoxin I5A [ 22 ] showed that ButaIT adopts a typical core structure of scorpion toxins primarily composed of one α-helix and three β-strands with four disulfide bridges, a feature similar to other toxins of similar size that act on K +and Cl -channels [ 17 31 34 38 ] . It is also evident from the data that disulfide bridge formation in ButaIT likely follows a common motif, with covalent links between cysl6-cys32, cys5-cys27, cys20-cys34 and an additional disulfide bridge between cys2 and cys 19 which cross-links the N-terminal strand of the β-sheet to the α-helix.
An examination of multiple sequence alignment with known insect toxins using BLAST search [ 28 ] revealed that ButaIT toxin shows considerable homology (Fig.
The molecular mass of ButaIT was determined using electrospray ionization mass spectrometry on a VG/Fisons Quattro-BD mass spectrometer (VG Biotech, Altrincham, UK).
Considering the high degree of sequence similarity, it is presumed that ButaIT will have a similar 3-D structure to that of other short toxins.