Table 2.
Physiochemical properties of most potent African Catfish Antimicrobial Peptides (ACAPs).
| Seq. ID. | Sequences | L | Charge | MW | α-helix (%) | H (%) | AS | Processor protein |
|---|---|---|---|---|---|---|---|---|
| ACAP-I | AALKKALTAGGY | 12 | 2 | 1163.68 | 58.30 | 75.00 | 0.905 | H15 domain-containing protein |
| ACAP-II | AALKKALAAGGY | 12 | 2 | 1133.67 | 66.67 | 83.33 | 0.898 | H15 domain-containing protein |
| ACAP-III | GVASAPASGTGGFSFG | 16 | 0 | 1369.64 | 0.00 | 75.00 | 0.768 | Uncharacterized |
| ACAP-IV | KVSKVLHKAIL | 11 | 3.5 | 1235.82 | 45.45 | 54.54 | 0.754 | SERPIN domain-containing protein |
| ACAP-V | VVLGSGGVGKSAL | 13 | 1 | 1143.67 | 0.00 | 76.92 | 0.684 | Small monomeric GTPase |
| ACAP-VI | FGGAGVGKTVL | 11 | 1 | 1005.57 | 0.00 | 81.81 | 0.677 | ATP synthase subunit beta |
| ACAP-VII | IAIIPSKKLRNKIAG | 15 | 4 | 1622.05 | 46.67 | 60.00 | 0.561 | 40S ribosomal protein |
L, peptide length; MW, molecular weight; H, hydrophobicity; and AS, antimicrobial score.