Table 1. Peptides used in the truncation study.
| Name | Sequence |
| 15-0 | (NH2)-SWFPLRSGGGS-(CONH2) |
| 15-1 | (NH2)-SWFPLRSGGG-(CONH2) |
| 15-2 | (NH2)-SWFPLRSGG-(CONH2) |
| 15-3 | (NH2)-SWFPLRSG-(CONH2) |
| 15-4 | (NH2)-SWFPLRS-(CONH2) |
| 15-5 | (NH2)-SWFPLR-(CONH2) |
| 15-6 | (NH2)-SWFPL-(CONH2) |
| 15-7 | (NH2)-SWFP-(CONH2) |
| 15-8 | (NH2)-WFP-(CONH2) |
| 15-9* | (NH2)-WFPLRSGGGS-(CONH2) |
| 15-10 | (NH2)-WFPLRSGGG-(CONH2) |
| 15-11 | (NH2)-WFPLRSGG-(CONH2) |
| 15-12 | (NH2)-WFPLRSG-(CONH2) |
| 15-13 | (NH2)-WFPLRS-(CONH2) |
| 15-14 | (NH2)-WFPLR-(CONH2) |
| 15-15 | (NH2)-WFPL-(CONH2) |
| 15-16 | (NH2)-SWAPLRSGGGS-(CONH2) |
Shown are all possible truncation combinations of peptide15, while still retaining the WFP motif. Each structure is given a number. The peptide15 lead structure has the number 15-0. Structure 15-9 was too hydrophobic for synthesis.