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. 2020 Jun 18;9(6):337. doi: 10.3390/antibiotics9060337

Table 1.

Examples of recently developed (2013–2020) natural and chemically modified Antimicrobial peptides (AMPs) against Tb.

Natural Peptides
AMP Chemical Structure Source Activity Mechanism of Action (MOA)
Pantocin wh-1 [22] Cycle Pantoea dispersa W18 Mycobacterium smegmatis mc2 155, H37Ra mice Unknown
Lassomycin [29] Cycle Lentzea kentuckyensis Mtb and Mycobacterium avium subsp. paratuberculosis. ATP-protease ClpC1P1P2
Bacteriocin AS-48 [30] Cycle Enterococcus faecalis H37Rv, H37Ra, BCG Pasteur 1173, Mt103, CDC1551, GC 1237, H37Rv phoP, SS18b, M. smegmatis mc2 155 Disruption of cell membranes
Micrococcin P1 [35] Thio-cycle Staphylococci H37Rv Inhibition of protein synthesis
Teixobactin [36] Iso-cycle Eleftheria terrae (β-proteobacterium) H37Rv Inhibition of cell wall synthesis
Ecumicin [37] Cycle Nonomuraea spp. MJM5123 H37Rv Inhibition of ClpC1
Rufomycin I/Ilamycin A [38] Cycle Streptomyces sp. (MJM3502), Streptomyces atratus (NRRL B-16927) Mtb and Mycobacterium abscessus Inhibition of ClpC1
Synthetic Peptides
Several cationic antimicrobial peptides (CAMPs) [23] Cationic peptide rich in W and R Peptide libraries M. smegmatis mc2 6, H37Rv and Mycobacterium tuberculosis lux strain Pore formation
Cinnamic acid (Cin+) CAMP1, 2, 3, 5, 7 [24] N-terminally modified protein Five de novo proteins designed from CAMPs [23] H37Rv, Multi drug resistant Tubercolosis (MDR-Tb) Pore formation
hBD consensus hBD10 [25] Disulfide bonds Human β-defensin (hBD) Multi drug resistant (MDR) strains, H37Rv Possible activity on Kv channels
NZX [26] Cysteine-rich protein Plectasin BCG, H37Rv Unknown
Vaejovis punctatus Antimicrobial peptide (VpAmp1.0, 2.0) [27] Cycle, disulfide bond Mexican scorpion Vaejovis punctatus MDR strains, H37Rv Cell lysis
Cyclohexyl griselimycin (CGM) [28] Cycle H37Rv, M. smegmatis mc2 155, Inhibition of dnaN
Vesicle associated membrane proteins (VAMP) α1, α2, α4 (VapBC30) [39] α-helix Fragments of VapBC30 H37Rv Inhibition of VapB30/VapC30
d-LAK 120 [40] D-amino acid derivative, α-helix MDR strains

  • Pore formation

  • Inhibition of protein synthesis
LL37-analogous peptide(LLAP) [41] LL-37 M. smegmatis Inhibition of ATPase
Synthetic AMPs (SAMPs-Dma) [42] Dimethylamination and imidazolation De novo designed M. smegmatis mc2 155

  • Cell penetration

  • DNA binding
Innate defense regulators ((IDR)-1002, -HH2, IDR-1018) [43,44,45] Macrophage chemotactic protein-1 (MCP-1) H37Rv, MDR strains

  • Immunomodulation

  • Anti-inflammation
RNAse (RN3) (1–45)
(RN6) (1–45)
(RN7) (1–45) [46,47]		 RNAse (RN)N-terminus Mycobacterium vaccae; Mycobacterium aurum; M. smegmatis mc2 155; Mycobacterium bovis; bacillus Calmette-Guérin (BCG)

  • Disruption of cell walls

  • Cell agglutination

  • Macrophage killing
Peptide B (Pep-B) [48] hBD-1 (H β-Defensin-1) H37Rv

  • Disruption of cell membranes

  • Increase in host immunity
Synthetic cyclomarin A [49,50] Cycle Cyclomarin A M. smegmatis, H37Rv ClpC1 activity inhibition
Pandinin-2 (Pin2) based [51] Short helix Pandinin-2 H37Rv Disruption of cell membranes