Table 1. Primary structures of HBD4 and the analogs with net charge at neutral pH.
| Peptide | Sequence | Net Charge |
|---|---|---|
| HBD4 a | ELDRIC 1GYGTAR C 2 RKK C 3 RSQEYRIGR C 4PNTYAC 5 C 6LRK | +7 |
| H4-1d b | EFELDRIC 1 Acm C 2 tBuGYGTAR C 3 RKKRSQEYRIGR C 4 tBuPNTYAC 5 Acm C 6LRK | +6 |
| H4-2d | EFELDRIC 1 C 2 tBuGYGTAR C 3 RKKRSQEYRIGR C 4 tBuPNTYAC 5 C 6LRK | +6 |
| H4-3d | EFELDRIC 1 C 2GYGTAR C 3 RKKRSQEYRIGR C 4PNTYAC 5 C 6LRK | +6 |
| H4-1dΔEF | ELDRIC 1 Acm C 2 tBuGYGTAR C 3 RKKRSQEYRIGR C 4 tBuPNTYAC 5 Acm C 6LRK | +7 |
| H4-1d[S] | EFELDRISSGYGTAR C 3 RKKRSQEYRIGR SPNTYASC 6LRK | +6 |
| H4-1d[S]ΔEF | ELDRISSGYGTAR C 3 RKKRSQEYRIGR SPNTYASC 6LRK | +7 |
a The HBD4 sequence corresponds to the commercially obtained synthetic peptide. The additional EF sequence in analogs corresponds to the start of the mature region of preproHBD4 protein sequence [17].
b Disulfide connectivity in H4-1d, H4-1dΔEF, H4-1d[S] and H4-1d[S]ΔEF is C3-C6. Disulfide connectivities in H4-2d are C2-C4 and C3-C6. Disulfide connectivities in HBD4 and H4-3d are C1-C5, C2-C4, and C3-C6. Side chain protecting groups acetamidomethyl (Acm) and tertiary-butyl (tBu) are shown by subscripts adjacent to cysteines respectively. Cationic residues are underlined.