Table 1.
Select antimicrobial peptides, amino acid sequences and properties1
| Class | Peptide | Amino acid sequence | Length | Net charge | Pho | Boman index | Source | APD ID |
|---|---|---|---|---|---|---|---|---|
| I | Gramicidin A | VGALAVVVWLWLWLW | 15 | 0 | 93% | −3.3 | Bacteria | 499 |
| Magainin 2 | GIGKFLHSAKKFGKAFVGEIMNS | 23 | +3 | 43% | 0.41 | Amphibians | 144 | |
| LL-37 (cathelicidin) | LLGDFFRKSKEKIGKEFKRIVQRIKFLRNLVPRTES | 37 | +6 | 35% | 3.0 | human | 310 | |
| Pyrrhocoricin (PrAMP) | VDKGSYLPRPTPPRPIYNRN | 20 | +3 | 15% | 3.2 | insects | 170 | |
| II | Nisin A (lantibiotic) | ITSISLCTPGCKTGALMGCNMKTATCHCSIHVSK | 34 | +3 | 44% | 0.37 | Bacteri | 205 |
| HNP1 (α-defensin) | ACYCRIPACIAGERRYGTCI YQGRLWAFCC | 30 | +3 | 53% | 1.1 | Human | 176 | |
| TAP (β-defensin) | NPVSCVRNK GICVPIRCPGSMKQIGTCVGRAVKCCRKK | 38 | +9 | 42% | 1.7 | Bovine | 235 | |
| Plectasin | GFGCNGPWD EDDMQCHNH CKSIKGYKGGYCAKGGFVCKCY | 40 | +1 | 32% | 1.4 | Fungi | 549 | |
| III | Colistin | XTXXKLLXXT | 10 | +6 | 20% | 2.9 | Bacteria | 2204 |
| Daptomycin | WNDTGKDADGSEY | 13 | −3 | 15% | 3.5 | Bacteria | 2203 | |
| Microcin J25 (bacteriocin) | VGIGTPIFSYGGGAGHVPEYF | 21 | −1 | 33% | −0.64 | Bacteria | 480 | |
| Alamethicin (peptaibol) | PBABAQBVBGLBPVBBEQ | 18 | −1 | 66% | −0.68 | Fungi | 2197 | |
| IV | Gramicidin S | VKLFPVKLFP | 10 | 2 | 60% | −1.3 | Bacteria | 2243 |
| Subtilosin A (bacteriocin) | NKGCATCSIGAACLVDGPIPDFEIAGATGLFGLWG | 35 | −2 | 51% | −0.46 | bacteria | 928 | |
| Kalata B1 (cyclotide) | GLPVCGETCVGGTCNTPG CTCSWPVCTRN | 29 | 0 | 37% | 0.67 | Plants | 729 | |
| RTD-1 (θ-defensin) | GFCRCLCRRGVCRCICTR | 18 | 5 | 55% | 2.8 | Monkey | 445 |
Data taken from the APD (http://aps.unmc.edu/AP), where Pho = hydrophobic%, B = α-aminoisobutyric acid and X = 2,4-diaminobutanoic acid. Boman index was originally called protein-binding potential by Boman [5]. Additional information, including the original reference, can be found in the APD. A unified peptide classification has been proposed [83] and adopted in the APD. This classification is based on the covalent bonding patterns of polypeptides. Class I (or UCLL) contains all linear peptides where both the backbone and sidechains may be modified but do not lead to a loop structure. Class II (or UCSS) contains peptides with a sidechain-sidechain connection, irrespective of intra or inter-connections. Class III (or UCSB) peptides must contain a covalent bond between backbone and sidechain, while class IV (or UCBB) consists of circular peptides due to a bond between backbone and backbone [83].