Review Article
Antimicrobial Peptides: Versatile Biological Properties
Table 2
List of antimicrobial peptides based on their structural features.
| Class of AMP | Structural features | Representative peptides | Structure | References |
| Cationic peptides | Peptides forming α-helical structures | Cecropins | α-Helix | [19] | Single disulphide bridge | Thanatin | β-Sheet | [20] | Two disulphide bridge | Tachyplesin II | β-Sheet | [21] | Three disulphide bridge | Penaeidins | β-Sheet | [22] | More than three disulphide bridge | Drosomycin | α β-Structure | [20] | Proline-rich peptide | Pyrrhocoricin | α β-Structure | [23] | Glycine-rich peptide | Diptericins | — | [24] | Histidine-rich peptide | Histatin | Rich in H | [25] | Tryptophan-rich peptide | Indolicidin | Extended | [26] |
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Noncationic peptides | Neuropeptide derived molecules | Secretolytin | α-Helix | [27] | Aspartic acid rich peptides | Dermcidin | — | [28] | Aromatic dipeptides | N-Alanyl-5-s-glutathionyl- 3,4 Dihydroxy-phenylalanine and p-hydroxy cinnamaldehyde | — | [29] | Oxygen binding proteins | Lactoferricin | β-Turn | [30] |
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