Table 2.

Microbe-derived bioactive peptides and their potential antimicrobial applications.

Name of the peptide	Microbial source	Target pathogen	Mode of action	References
Pediocins	Pediococcus spp.	Bacteria	Disrupt proton motive force, formation of pores in the cytoplasmic membrane, and cell membrane dysfunction	[69]
		Listeria monocytogenes
Nisin	Lactococcus lactis	Bacteria	Pore formation and the inhibition of cell wall biosynthesis	[70–72]
		Listeria monocytogenes
		Streptococcus aureus
		Spore-forming Bacillus Clostridium species
Lacticin 3147	Lactococcus lactis	Bacteria	Cell wall disruption and pore formation	[70]
		Staphylococcus aureus
		Enterococcus faecalis
		Pneumococcus
		Propionibacterium acnes, Streptococcus mutans, and Listeria monocytogenes
		Bacillus cereus
Enterocin A	Enterococcus faecium	Bacteria	Interacts with cell wall and cell receptor, membrane permeabilization causes the leakage, and interferes in DNA replication and mRNA synthesis and transcription	[72, 73]
		L. monocytogenes
		Staphylococcus aureus and Salmonella enterica
Propionicin	P. thoenii, P. jensenii, and P. freudenreichii	Bacteria	Unknown	[74, 75]
		Helicobacter pylori
		Listeria monocytogenes
		Corynebacterium spp.
		Vibrio parahaemolyticus
		Yersinia enterocolitica
		Pseudomonas spp.,
		Saccharomyces spp.
		Aspergillus spp.
		Fungi
		Aspergillus wentii and Apiotrichum curvatum
		Fusarium tricinctum and Phialophora gregata
		Candida, Saccharomyces, and Scopulariopsis genera
Lynronne	Rumen microbiome	Bacteria	Membrane permeabilization pore formation and lysis	[76, 77]
		Staphylococcus aureus
		Acinetobacter baumannii
		P. aeruginosa
Gramicidin S	Aneurinibacillus migulanus	Bacteria	Binding of peptides to Gram-negative LPS and their ability to disrupt Gram-negative cell membranes, accumulation of bacterial membrane phospholipids, and pore formation in the cell membrane	[78, 79]
		E. coli
		Klebsiella pneumoniae and Pseudomonas aeruginosa
		Acinetobacter baumannii Staphylococcus aureus
		Enterococcus faecium
Gramicidin A	Bacillus brevis	Bacteria	Membrane permeabilization, interruption of internal molecular function (DNA and protein functions), formation of hydroxyl free radicals, and the imbalance of NADH metabolism	[80, 81]
		Staphylococcus aureus
Gramicidin A (1)	Bacillus brevis	Bacteria	Disrupts the transmembrane ion concentration gradient by forming an ion channel in a lipid bilayer	[82]
		S. pyogenes and S. pneumoniae
		Enterococcus faecalis
		Streptococcus agalactiae
Endolysins (phage-derived AMP)	Bacteriophages of A. baumannii	Bacteria	Cause hydrolysis of bacterial cell wall	[83]
		Acinetobacter baumannii
		Fungi
		Aspergillus fumigatus
		Candida albicans
Tyrocidines	Bacillus aneurinolyticus	Bacteria	Binds to bacterial membranes and disrupts structural integrity, resulting in bacterial cell death, disruption of the asexual cycle of the parasite and inhibit the respiration of parasitized red cells	[84–87]
		B. Subtilis
		C. albicans
		Parasite
		Caenorhabditis elegans
		Plamodium gallinaceum
Valinomycin	Streptomyces cavourensis, S. fulvissimus, S. roseochromogenes, and S. griseus	Bacteria	Degradation of glycolytic ATP affects respiration and disrupts the K+ ion gradient across the cell membrane, and the unbalanced distribution of ions in the bacterium causes cell death and fungal cell wall and cell membrane permeabilization	[88–90]
		Streptococcus faecalis and Micrococcus lysodeikticus
		Staphylococcus aureus
		Fungi
		Candida albicans
		Cryptococcus albidus
Aureobasidin A 1 (cyclodepsipeptides)	Aureobasidium pullulans R106	Fungi	Affect spore germination rate, germination initiation, polarized growth of germ tube, and elongation rate; inhibit inositolphosphoryl-ceramide (IPC) synthase; inhibition of sphingolipid biosynthesis resulting in loss of intracellular structure and vacuolization; and membrane trafficking which disturbed cell proliferation of the parasite	[91]
		Penicillium digitatum
		P. italicum, P. expansum, Botrytis cinerea, and Monilinia fructicola
		C. albicans, S. cerevisiae, and C. neoformans
		A. fumigates, Schizosaccharomyces pombe, and A. nidulans
		A. Niger and A. oryzae
		Parasite
		Toxoplasma gondii
		Leishmania amazonensis
Colistin (polymyxin E)	Paenibacillus polymyxa	Bacteria	Increase the permeability of the bacterial membrane, leading to leakage of the cytoplasmic content and causing cell death, and bind to lipid portion A and neutralize and inhibit vital respiratory enzymes	[92]
		E. coli and A. baumannii
		P. aeruginosa and Stenotrophomonas maltophilia
		Enterobacter spp.
		Klebsiella spp.
		Citrobacter spp.
		Salmonella spp., and Shigella spp.
Omphalitis	Omphalotus olearius	Nematodes	Unknown	[93]
		Meloidogyne incognita and Caenorhabditis elegans
Daptomycin	Streptomyces roseosporus	Bacteria staphylococci and enterococci	Bacterial cell membrane, causing rapid membrane depolarization and a potassium ion efflux, followed by the arrest of DNA, RNA, and protein synthesis, resulting in bacterial cell death	[94, 95]
Pargamicin A	Amycolatopsis sp.	Bacteria	Disruption of the membrane potential, leading to loss of the membrane function	[94, 95]
		S. aureus and E. faecalis
Nocardithiocin	Nocardia pseudobrasiliensis	Bacteria	Cell membrane or cell wall permeability	[94, 96]
		Mycobacterium
		Gordonia species
		M. tuberculosis
Xylapeptide	Xylaria sp.	Bacteria	Unknown	[94]
		Bacillus subtilis
		B. cereus, B. megaterium, and Micrococcus luteus
		S. aureus and Shigella castellani
		Fungus
		C. albicans
Lugdunin	Staphylococcus lugdunensis	Bacteria	Impairment of membrane integrity or ion transport and proton leakage in synthetic, protein-free membrane vesicles	[94, 97, 98]
		Staphylococcus aureus and vancomycin-resistant Enterococcus
Venturamide	Oscillatoria sp.	Parasite	Unknown	[94]
		P. falciparum
Xenoamicin A	Xenorhabdus doucetiae and Xenorhabdus mauleonii	Parasite	Interacts with the cytoplasmic membrane	[94, 99]
		P. falciparum
		T. brucei rhodesiense
Szentiamide	Xenorhabdus szentirmaii	Parasite	Interacts with the cytoplasmic membrane	[99]
		Plasmodium falciparum
		Trypanosoma cruzi
		Bacteria
		M. luteus
Apicidin	Fusarium semitectum	Parasite	Inhibit histone deacetylase of parasite	[100, 101]
		Plasmodium falciparum and T. gondii
		Plasmodium berghei
Thiostrepton	Streptomyces azureus and Streptomyces laurentii	Parasite	Inhibition of protein synthesis by proteasome β subunits and inhibition of mRNA translation	[100]
		Plasmodium berghei
Amphomycin	Streptomyces canus	Parasite	Inhibits the biosynthesis of the glycolipid precursor of glycosylphosphatidylinositol (GPI) protein by which the variant surface glycoproteins (VSGs) are anchored in the membrane of the parasites	[100]
		Trypanosoma brucei
		T. b. gambiense
		T. b. rhodesiense
Leucinostatins (A and B) and alamethicin	Paecilomyces spp	Parasite	Pore formation in the membranes and interruption of cellular homeostasis, resulting in the death of the parasite	[100]
		Trypanosoma brucei
		T. b. brucei and T. b. rhodesiense
Haloduracin (lantibiotic)	Bacillus halodurans	Bacteria	Pore formation, cell membrane attack, and the inhibition of cell wall synthesis	[102]
		B. anthracis
		Vancomycin-resistant Enterococcus faecium, Bacillus cereus, and methicillin-resistant
		Staphylococcus aureus
Albicidin	Xanthomonas albilineans	Bacteria	Inhibit DNA replication, transcription, supercoiling, gene regulation, and catalytic DNA cleavage-religation cycle of the GyrA subunit	[103, 104]
		Enterobacter aerogenes
		Escherichia coli
		Haemophilus influenza
		Klebsiella pneumonia
		Shigella sonnei and Staphylococcus aureus
Griselimycin	Streptomyces griseus	Bacteria	Inhibit nucleic acid biosynthesis by sliding clamp of DNA polymerase III	[104, 105]
		Mycobacterium tuberculosis
Colicin E	Escherichia coli	Bacteria	Inhibit nucleic acid biosynthesis by cleaving the targeted cell's DNA or tRNA and digests the peptidoglycan precursors, leading to cell death pore formation in the inner membrane and degrade the internal molecular components	[71, 104, 106, 107]
		Shiga-toxin-producing E. coli
		Enteroinvasive
		E. coli and Shigella
		Enterobacter
		Klebsiella and Morganella
		Salmonella, Shigella, and Yersinia
Dudawalamides	Moorea producens	Parasite	Unknown	[94]
		P. falciparum, Trypanosoma cruzi, and Leishmania donovani
Ambobactin	Streptomyces ambofaciens	Bacteria	Target cytoplasmic membrane	[94, 108]
		Bacillus subtilis
		Escherichia coli
		Erwinia carotovora
		Pseudomonas syringae
		Fungi
		Ralstonia solanacearum and Xanthomonas oryzae
Teixobactin	Eleftheria terrae	Bacteria	Inhibits bacterial cell wall synthesis by binding to the precursor of peptidoglycan and teichoic acid	[94]
		S. aureus
		Streptococcus pneumonia, M. tuberculosis, Clostridium difficile, and Bacillus anthracis
Maribasins	Bacillus marinus	Fungi	Unknown	[109]
		Alternaria solani, Fusarium oxysporum, Rhizoctonia solani, and Verticillium albo-atrum
Clavariopsins	Clavariopsin aquatica	Fungi	Inhibit the synthesis of fungal cell walls	[91]
		C. albicans, Aspergillus fumigatus, and A. niger
Anidulafungin	Aspergillus oryzae	Fungi	Inhibition on β-(1,3)-glucan synthase	[109]
		Candida
GE81112	Streptomyces sp.	Bacteria	Inhibit bacterial protein synthesis machinery	[110]
		S. pneumoniae, E. faecalis, E. coli and B. subtilis, and S. pyogenes
Carmaphycin B	Symploca sp.	Parasite	Targets Plasmodium proteasome	[96]
		Plasmodium falciparum
Kakadumycin A	Streptomyces sp.	Bacteria	Binding to DNA prevents RNA synthesis	[111]
		Bacillus anthracis
		Enterococcus faecium, Staphylococcus simulans, and Staphylococcus aureus
		S. pneumonia
		Listeria monocytogenes
		Parasite
		Plasmodium falciparum
Fengycins	Bacillus subtilis	Fungi	Disrupt the mitochondrial membrane potential, production of reactive oxygen species, and chromatin condensation in fungal hyphal cells resulting in hyphal cell death	[112]
		Magnaporthe grisea
		Aspergillus niger
		Mucor rouxii
		Rhizopus stolonifer
		Gibberella zeae and Fusarium graminearum
		Sclerotinia sclerotiorum