Table 2.
Name of the group | Representative peptides | Origin | Structure | Mechanism | MW1 | Susceptible strain | References |
---|---|---|---|---|---|---|---|
Cecropins | 60 members; Cecropin A | Insects | α-helical Tryptophan in the first or second position; C- amidated end | Membrane lysis | 2800–4000 |
Aspergillus spp. Fusarium moniliforme Fusarium oxysporum |
Giacometti A et al, 2001; (121) De Lucca A et al, 1988; (124) |
Magainins | Magainin 2 | Frogs | α-helical Rich in glycine and serine amino acids | Membrane lysis; DNA damage | 2500–3000 |
C. albicans C. neoformans Saccharomyces cerevisiae |
Zasloff M 1987(111); Morton C et al, 2007(114) |
Bombinin-like and bombinin H | BLP-1,3 Bombinins H1-7 |
α-helical Glycine-rich; C- terminal amino acid amidated | Membrane lysis | 2300–4000 |
C. albicans C. guillermondii C. tropicalis |
Simmaco M et al, 2009(137) | |
Dermaseptins | Dermaseptin S1-5 | α-helical Lysine-rich | Membrane lysis; Apoptosis induction | 2500–3500 | A. fugimatus | Mor A et al, 1991(112); Morton C et al, 2007(114) | |
Cathelicidins (without cysteines) | LL-37; mCRAMP; BMAP-27–28 | Humans, cattle, pigs, goats, mice | α-helical | Membrane lysis | 3000–4000 |
C. albicans C. neoformans |
Boman H et al, 2003(279); Benincasa M et al, 2006(160) |
Indolicin; Tritrpticin | Extended wedge Rich in tryptophans | Membrane lysis | 1900–2000 |
C. neoformans Candida spp. A. fumigatus |
|||
PA26 | PA26 | Combinatori al Library | Penatratin-like hexapeptide | Unknown | 950 | Penicillum digitatum, S. cerevisiae | Munoz A et al, 2006(280) |
Kaxins | dF21-10K | Synthetic design | Non-amphipathic hydrophobic core N-terminal lysine-rich | Membrane- lysis | 1830–2350 | Candida spp. | Burrows H et al, 2006 (175) |
Thanatin | Thanatin | β-sheet, single disulfide bond forming C- terminal | Membrane lysis | 2400 |
A. fumigatus N. crassa T. mentagrophytes |
Fehlbaum P et al, 1996(176); Bulet P et al, 1999(281) | |
Cathelicidins (with cysteines) | Protegrins1-5 | Pigs | β-sheet, 2 disulfide bridges | Membrane lysis | 1900–2200 | C. albicans | Kokryakov V et al, 1993 (282) |
α-Defensins | HNP1-4; HD5-6; NP-1 | Mammals | Cyclic: 3, Disulfide bridges C1-6, C2-4, C3-5 | Membrane lysis | 3000–4000 |
Candida spp. A. fumigatus C. neoformans |
Ganz T et al, 2002 (30); Lehrer RI 2004(283); Levitz S et al, 1986(202) |
β-Defensins | HBD1-4 Bovine tracheal antimicrobial peptide | Mammals | Cyclic: Disulfide bridges C1-5, C2-4, C3-6 | Membrane lysis | 3500–5000 |
Candida spp A. fumigatus |
Diamond G et al, 1991 (224); Joly S et al, 2004(222) |
θ-Defensins | rTD1-3 | Rhesus monkeys | Circular octadecapeptides, 2 anti-parallel β-sheets and 3 disulfide bonds | Membrane lysis | 2100 |
C. albicans C. neoformans |
Tang, YQ et al, 1999 (20); Tran, D et al, 2008(225) |
Gallinacins | Gallinacin-1 and 1 α, gallinacin-2 and -6 | Chicken | β-sheet, rich in lysine and arginine, 3 disulphide bonds | Membrane lysis combined with effect on DNA replication, RNA and protein synthesis | 2000–5000 |
C. albicans S. cereviseae |
Van Dijk A et al, 2007(227) |
Macrocycles | Kalata Circulin A,B Cyclopsychotride | Plants | Cyclic knot | Membrane lysis | 2800–3400 |
C. kefyr C. tropicalis |
Tam J et al 1999(228), |
Syringomycins Pseudomycins | Syringomycin E Syringotoxin B Syringostatin A |
Bacteria | Lipodepsinonapeptides | Membrane lysis | 2300–3500 |
Candida spp Aspergillus |
Feigin A et al, 1996(229); Sorensen K et al, 1996(231) |
Lactoferrin2- dervived peptides | Peptide 2 Lactoferricin | Mammals | Glycosylated protein, two symmetrical lobes (N and C lobes), mixture of α-helix and β-sheet | Membrane lysis | 2600–4660 | C. albicans Crypt. albidus,, Dekkera bruxellensis, Pichia membranifaciens, Saccharomyces cerevisiae, Zygosaccharomyce s bisporus | Gonzalez- Chavez S et al, 2009(284) Ueta E et al; 2001;(242) Viejo-Diaz, M. et al, 2005 #4524}(241) |
BPI protein2 domain III analogs | XMP.284 XMP. 366 XMP.391 |
Lipid binding protein; the amino-terminal rich in lysine residues | Membrane lysis | 1550 |
Candida spp C. neoformans A. fumigatus Histoplasma capsulatum |
Elsbach, P. et al, 2003(245) |
MW, approximate molecular weight;
The molecular weights of lactoferrin and BPI are 55000 and 80000, respectively