Table 3.
List of hydrocarbon stapled antimicrobial peptides studied in articles cited in this review (part 1)
| Article title | Peptide | Peptide sequences | Ref. |
|---|---|---|---|
| Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera | Lasioglossin III analogs | [35] | |
| LL-IIIs-1 | VNWKKXLGKXIKVVK-NH2 | ||
| LL-IIIs-2 | VNWKKILGKXIKVXK-NH2 | ||
| LL-IIIs-3 | VXWKKXLGKIIKVVK-NH2 | ||
| LL-IIIs-4 | VNX1KKIX1GKX2IKVX2K-NH2 | ||
| LL-IIIs-5 cis | VNXKKILGKXIKVVK-NH2 cis | ||
| LL-IIIs-5 trans | VNXKKILGKXIKVVK-NH2 trans | ||
| LL-IIIs-6 a | VNX1KKIX1PKX2IKVX2K-NH2 a | ||
| LL-IIIs-6 b | VNX1KKIX1PKX2IKVX2K-NH2 b | ||
| Melectin analogs | |||
| MEP-Ns-1 | GFLSILKKVLPKXNleAHXK-NH2 | ||
| MEP-Ns-2 | GFLSXLKKXLPKVNleAHNleK-NH2 | ||
| MEP-Ns-3 | GFLSX1LKKX1LPKX2NleAHX2K-NH2 | ||
| MEP-Ns-4 cis | GFXSILKKVXPKVNleAHNleK-NH2 cis | ||
| MEP-Ns-4 trans | GFXSILKKVXPKVNleAHNleK-NH2 trans | ||
| MEP-Ns-5 | GFLSX1LKKX1LGKX2NleAHX2K-NH2 | ||
| MEP-Ns-5x | GFLSX0LKKX1LGKX1NleAHX0K-NH2 | ||
| MEP-Ns-6 | GFLSX1LKKX1LAKX2NleAHX2K-NH2 | ||
| MEP-Ns-6x | GFLSX0LKKX1LAKX1NleAHX0K-NH2 | ||
| Truncated and constrained helical analogs of antimicrobial esculentin-2EM | E2EM15W-S1 | Ac-TLKQFXKGVXKWLVK-NH2 | [36] |
| E2EM15W-S2 | Ac-TLKQFXKGWXKDLVK-NH2 | ||
| E2EM15W-S3 | Ac-TLKQWXKGVXKDLVK-NH2 | ||
| De novo design and their antimicrobial activity of stapled amphipathic helices of heptapeptides | S1 | Ac-KXWKAXK-NH2 | [37] |
| S2 | Ac-KXAKWXK-NH2 | ||
| S3 | Ac-KXWKLXK-NH2 | ||
| S4 | Ac-KXLKWXK-NH2 | ||
| S5 | Ac-KXWAKXA-NH2 | ||
| S6 | Ac-KXAWKXA-NH2 | ||
| N-Capping effects of stapled heptapeptides on antimicrobial and hemolytic activities | H-S1 | KXWKAXK-NH2 | [38] |
| H-S2 | KXAKWXK-NH2 | ||
| H-S3 | KXWKLXK-NH2 | ||
| H-S4 | KXLKWXK-NH2 |
X stands for Cα-methyl, Cα-alkenyl amino acid residues (1, 2—stapled; 0—unstapled); a, b—two not identified isomers