Table 3.
Alignment of the primary structures of the novel antimicrobial peptides, AaeAP1 and AaeAP2, with scorpion venom homologues present in the NCBI database. Note that AaeAP1 and AaeAP2 are both nonadecapeptides, and the majority of homologues are octadecapeptides. Note also that all peptides are C-terminally amidated (a). Identical residues are represented by dashes.
| Species | Peptide | Primary structure | Nucleotide sequence database |
|---|---|---|---|
| Androctonus aeneas | AaeAP1 | FLFSLIPSVIAGLVSAIRNa | (Accession No. HG792997) |
| Androctonus aeneas | AaeAP2 | --------A----------a | (Accession No. HG792998) |
| Mesobuthus martensii | Kb1 | --------A-S--I--FKa | (Accession No. AF159979) |
| Mesobuthus eupeus | caerin-like AMP | --------A-S--I--FKa | (Accession No. KC108907) |
| Androctonus amoreuxi | AamAP1 | -------HA-G--I--FKa | (Accession No. FR821613) |
| Isometrus maculatus | imcroporin | -F---L--L-G------Ka | (Accession No. FJ750949) |
| Lychas mucronatus | mucroporin | --G----L-G-----FKa | (Accession No. EU669864) |
| Mesobuthus martensii | BmKb2 | --S-----A-S--I--FKa | (Accession No. AF543048) |
| Tityus costatus | AMP clone 5 | -F------L-G---F--Ka | (Accession No. AY740687) |
| Androctonus amoreuxi | AamAP2 | -P-----HA-GG-ISAIKa | (Accession No. FR821614) |