Two amphiphilic peptides with the following sequences were designed an
d synthesised: peptide 1, TFLQDLKEKVQQLTEALK; peptide 2, TVSQLQEYWTTLL
SQIKTLLQQIKTS. The emulsification properties of these peptides were te
sted in an oil-water two-phase system and were found to be significant
ly greater than those of mellitin. Circular dichroism measurements wer
e used to characterise the secondary structure of the peptides. In aqu
eous buffer, they adopted c. 50% beta sheet conformation.