Table 5.
Post-translational modifications of natural antimicrobial peptides
| Search key | Post-translational modification |
Peptide count |
|---|---|---|
| XXA | Amidation | 448 |
| XXB | Chromophore/ion-binding moieties |
4 |
| XXC | Backbone cyclization | 176 |
| XXD | D-amino acids | 17 |
| XXE | Acetylation | 11 |
| XXF | Carboxylic-acid-containing unit |
8 |
| XXG | Glycosylation | 12 |
| XXH | Halogenation (Cl, Br) | 8 |
| XXJ | Sidechain-backbone cyclization |
15 |
| XXK | Hydroxylation | 9 |
| XXL | Lipidation | 9 |
| XXM | Methylation | 3 |
| XXN | Nitrolation | 0 |
| XXO | Oxidation | 10 |
| XXP | Phosphorylation | 3 |
| XXQ | N-terminal cyclic glutamate | 15 |
| XXR | Reduction | 2 |
| XXS | Sulfation | 1 |
| XXT | Thioether bridge | 46 |
| XXU | Rana Box via a single S-S bond |
269 |
| XXW | Dehydration | 21 |
| XXY | Citrullination | 1 |
| Structure searcha |
Disulfide bridges | 551 |
a
This number was obtained by searching for disulfide bond-containing AMPs classified as “Bridge”, “β structure”, and “αβ structure” families, respectively. The “bridged” AMPs are known to have disulfide bonds but unknown 3D structure. Beta structures without disulfide bonds were excluded by including “c” as a sequence search term. For the αβ structures, only the AMPs with a packed 3D fold were counted.