Two amphiphilic, synthetic peptides display strong emulsification properties

Abstract Two amphiphilic peptides with the following sequences were designed and synthesised: peptide 1, TFLQDLKEKVQQLTEALK; petide 2, TVSQLQEYWT-TLLSQIKTLLQQIKTS. The emulsification properties of these peptides were tested in an oil-water two-phase system and were found to be significantly greater than those of mellitin. Circular dichroism measurement were used to characterise the secondary structure of the peptides. In aqueous buffer, they adopted c . 50% beta sheet conformation.