{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T17:53:12Z","timestamp":1790790792981,"version":"4.1.0"},"reference-count":147,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2021,6,5]],"date-time":"2021-06-05T00:00:00Z","timestamp":1622851200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Harmful fungi in nature not only cause diseases in plants, but also fungal infection and poisoning when people and animals eat food derived from crops contaminated with them. Unfortunately, such fungi are becoming increasingly more resistant to traditional synthetic antifungal drugs, which can make prevention and control work increasingly more difficult to achieve. This means they are potentially very harmful to human health and lifestyle. Antifungal peptides are natural substances produced by organisms to defend themselves against harmful fungi. As a result, they have become an important research object to help deal with harmful fungi and overcome their drug resistance. Moreover, they are expected to be developed into new therapeutic drugs against drug-resistant fungi in clinical application. This review focuses on antifungal peptides that have been isolated from bacteria, fungi, and other microorganisms to date. Their antifungal activity and factors affecting it are outlined in terms of their antibacterial spectra and effects. The toxic effects of the antifungal peptides and their common solutions are mentioned. The mechanisms of action of the antifungal peptides are described according to their action pathways. The work provides a useful reference for further clinical research and the development of safe antifungal drugs that have high efficiencies and broad application spectra.<\/jats:p>","DOI":"10.3390\/molecules26113438","type":"journal-article","created":{"date-parts":[[2021,6,6]],"date-time":"2021-06-06T23:59:55Z","timestamp":1623023995000},"page":"3438","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":117,"title":["Activity and Mechanism of Action of Antifungal Peptides from Microorganisms: A Review"],"prefix":"10.3390","volume":"26","author":[{"given":"Tianxi","family":"Li","sequence":"first","affiliation":[{"name":"College of Animal Science & Veterinary Medicine, Shenyang Agricultural University, Shenyang 110866, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lulu","family":"Li","sequence":"additional","affiliation":[{"name":"College of Animal Science & Veterinary Medicine, Shenyang Agricultural University, Shenyang 110866, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fangyuan","family":"Du","sequence":"additional","affiliation":[{"name":"College of Animal Science & Veterinary Medicine, Shenyang Agricultural University, Shenyang 110866, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lei","family":"Sun","sequence":"additional","affiliation":[{"name":"College of Animal Husbandry and Veterinary Medicine, Jinzhou Medical University, Jinzhou 121001, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jichao","family":"Shi","sequence":"additional","affiliation":[{"name":"Liaoning Agricultural Development Service Center, Shenyang 110032, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6683-1956","authenticated-orcid":false,"given":"Miao","family":"Long","sequence":"additional","affiliation":[{"name":"College of Animal Science & Veterinary Medicine, Shenyang Agricultural University, Shenyang 110866, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zeliang","family":"Chen","sequence":"additional","affiliation":[{"name":"College of Animal Science & Veterinary Medicine, Shenyang Agricultural University, Shenyang 110866, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,6,5]]},"reference":[{"key":"ref_1","first-page":"64","article-title":"Reduction of the content of aflatoxin-forming fungi in contaminated grains by methods of hydrothermal treatment","volume":"94","author":"Shentsova","year":"2015","journal-title":"Gig. I Sanit."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1093\/cid\/ciy859","article-title":"Voriconazole Resistance and Mortality in Invasive Aspergillosis: A Multicenter Retrospective Cohort Study","volume":"68","author":"Lestrade","year":"2019","journal-title":"Clin. Infect. Dis. Off. Publ. Infect. Dis. Soc. Am."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"3578","DOI":"10.1128\/AAC.00303-10","article-title":"A clinical isolate of Candida albicans with mutations in ERG11 (encoding sterol 14alpha-demethylase) and ERG5 (encoding C22 desaturase) is cross resistant to azoles and amphotericin B","volume":"54","author":"Martel","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/2008-2231-21-1","article-title":"Overexpression of aldo-keto-reductase in azole-resistant clinical isolates of Candida glabrata determined by cDNA-AFLP","volume":"21","author":"Farahyar","year":"2013","journal-title":"Daru J. Fac. Pharm. Tehran Univ. Med. Sci."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"464","DOI":"10.3389\/fmicb.2017.00464","article-title":"Notable Increasing Trend in Azole Non-susceptible Candida tropicalis Causing Invasive Candidiasis in China (August 2009 to July 2014): Molecular Epidemiology and Clinical Azole Consumption","volume":"8","author":"Fan","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1126\/science.aap7999","article-title":"Worldwide emergence of resistance to antifungal drugs challenges human health and food security","volume":"360","author":"Fisher","year":"2018","journal-title":"Science"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.3390\/ph6121543","article-title":"Antimicrobial peptides","volume":"6","author":"Bahar","year":"2013","journal-title":"Pharmaceuticals"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1038\/292246a0","article-title":"Sequence and specificity of two antibacterial proteins involved in insect immunity","volume":"292","author":"Steiner","year":"1981","journal-title":"Nature"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1089\/sur.2018.194","article-title":"Antimicrobial Peptides","volume":"19","author":"Fry","year":"2018","journal-title":"Surg. Infect."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"539","DOI":"10.3181\/00379727-67-16367","article-title":"Bacillomycin: An antibiotic from Bacillus subtilis active against pathogenic fungi. Proceedings of the Society for Experimental Biology and Medicine","volume":"67","author":"Landy","year":"1948","journal-title":"Soc. Exp. Biol. Med."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1128\/jb.86.3.387-391.1963","article-title":"Mode of action of mycobacillin, a new antifungal antibiotic","volume":"86","author":"Banerjee","year":"1963","journal-title":"J. Bacteriol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.1128\/jb.87.6.1397-1401.1964","article-title":"Biosynthesis of mycobacillin, a new antifungal peptide. i. role of nucleic acid","volume":"87","author":"Banerjee","year":"1964","journal-title":"J. Bacteriol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/0092-8674(91)90154-Q","article-title":"Antibacterial peptides: Key components needed in immunity","volume":"65","author":"Boman","year":"1991","journal-title":"Cell"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Li, X., Zhang, Y., Wei, Z., Guan, Z., Cai, Y., and Liao, X. (2016). Antifungal Activity of Isolated Bacillus amyloliquefaciens SYBC H47 for the Biocontrol of Peach Gummosis. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0162125"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2459","DOI":"10.1002\/hlca.19740570818","article-title":"Metabolites of microorganisms. 143. Echinocandin B, a novel polypeptide-antibiotic from Aspergillus nidulans var. echinulatus: Isolation and structural components","volume":"57","author":"Nyfeler","year":"1974","journal-title":"Helv. Chim. Acta"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.micres.2013.07.014","article-title":"Pharmaceutically active secondary metabolites of marine actinobacteria","volume":"169","author":"Manivasagan","year":"2014","journal-title":"Microbiol. Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.peptides.2018.03.011","article-title":"Actinobacteria-Derived peptide antibiotics since 2000","volume":"103","author":"Zhao","year":"2018","journal-title":"Peptides"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/S0213-005X(08)76587-X","article-title":"In vitro activity of anidulafungin. Comparison with the activity of other echinocandins","volume":"26","year":"2008","journal-title":"Enferm. Infecc. y Microbiol. Clin."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.ejmech.2012.01.054","article-title":"Total synthesis and structure-activity relationships of new echinocandin-like antifungal cyclolipohexapeptides","volume":"50","author":"Yao","year":"2012","journal-title":"Eur. J. Med. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Zhao, Y., and Perlin, D.S. (2020). Review of the Novel Echinocandin Antifungal Rezafungin: Animal Studies and Clinical Data. J. Fungi, 6.","DOI":"10.3390\/jof6040192"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2710","DOI":"10.1128\/AAC.40.12.2710","article-title":"In vitro antifungal and fungicidal activities and erythrocyte toxicities of cyclic lipodepsinonapeptides produced by Pseudomonas syringae pv. syringae","volume":"40","author":"Sorensen","year":"1996","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/s11274-017-2392-5","article-title":"Two novel cationic antifungal peptides isolated from Bacillus pumilus HN-10 and their inhibitory activity against Trichothecium roseum","volume":"34","author":"Yan","year":"2018","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/j.micres.2013.03.001","article-title":"Isolation and identification of antifungal peptides from Bacillus BH072, a novel bacterium isolated from honey","volume":"168","author":"Zhao","year":"2013","journal-title":"Microbiol. Res."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"256","DOI":"10.4014\/jmb.1107.07021","article-title":"Isolation and characterization of Bacillus sp. producing broad-spectrum antibiotics against human and plant pathogenic fungi","volume":"22","author":"Chen","year":"2012","journal-title":"J. Microbiol. Biotechnol."},{"key":"ref_25","first-page":"1494","article-title":"Antifungal mechanism of Bacillus marinus B-9987","volume":"49","author":"Gao","year":"2009","journal-title":"Wei Sheng Wu Xue Bao = Acta Microbiol. Sin."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"4377","DOI":"10.1007\/s00253-019-09805-z","article-title":"Capability of iturin from Bacillus subtilis to inhibit Candida albicans in vitro and in vivo","volume":"103","author":"Lei","year":"2019","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/BF00436368","article-title":"Inhibition of some mycotoxigenic fungi by iturin A, a peptidolipid produced by Bacillus subtilis","volume":"116","author":"Klich","year":"1991","journal-title":"Mycopathologia"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1186\/2193-1801-2-543","article-title":"A novel antifungal protein of Bacillus subtilis B25","volume":"2","author":"Tan","year":"2013","journal-title":"SpringerPlus"},{"key":"ref_29","first-page":"778","article-title":"Antagonism against Beauveria bassiana by lipopeptide metabolites produced by entophyte Bacillus amyloliquefaciens strain SWB16","volume":"54","author":"Wang","year":"2014","journal-title":"Wei Sheng Wu Xue Bao = Acta Microbiol. Sin."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1007\/s00284-002-3955-7","article-title":"An antifungal chitinase produced by Bacillus cereus with shrimp and crab shell powder as a carbon source","volume":"47","author":"Chang","year":"2003","journal-title":"Curr. Microbiol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1016\/j.biortech.2006.05.005","article-title":"Antifungal activity and enhancement of plant growth by Bacillus cereus grown on shellfish chitin wastes","volume":"98","author":"Chang","year":"2007","journal-title":"Bioresour. Technol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"39","DOI":"10.2174\/0929866521666140901143114","article-title":"Heterologous expression of the antifungal \u03b2-chitin binding protein CBP24 from bacillus thuringiensis and its synergistic action with bacterial chitinases","volume":"22","author":"Mehmood","year":"2015","journal-title":"Protein Pept. Lett."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1016\/j.ijbiomac.2019.12.216","article-title":"Identification and characterization of a serine protease from Bacillus licheniformis W10: A potential antifungal agent","volume":"145","author":"Ji","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/j.synbio.2019.08.002","article-title":"Depiction of secondary metabolites and antifungal activity of Bacillus velezensis DTU001","volume":"4","author":"Devi","year":"2019","journal-title":"Synth. Syst. Biotechnol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"129","DOI":"10.7164\/antibiotics.49.129","article-title":"Fusaricidin A, a new depsipeptide antibiotic produced by Bacillus polymyxa KT-8. Taxonomy, fermentation, isolation, structure elucidation and biological activity","volume":"49","author":"Kajimura","year":"1996","journal-title":"J. Antibiot."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3990","DOI":"10.1007\/s00284-020-02206-w","article-title":"Isolation and Characterization of a New Fusaricidin-Type Antibiotic Produced by Paenibacillus bovis sp. nov BD3526","volume":"77","author":"Hua","year":"2020","journal-title":"Curr. Microbiol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1002\/jobm.201400505","article-title":"Isolation and characterization of an antimicrobial lipopeptide produced by Paenibacillus ehimensis MA2012","volume":"55","author":"Naing","year":"2015","journal-title":"J. Basic Microbiol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1016\/j.peptides.2003.08.021","article-title":"Prevention of lethal murine candidiasis using HP (2-20), an antimicrobial peptide derived from the N-terminus of Helicobacter pylori ribosomal protein L1","volume":"24","author":"Ribeiro","year":"2003","journal-title":"Peptides"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"4507","DOI":"10.1073\/pnas.1620432114","article-title":"Enterococcus faecalis bacteriocin EntV inhibits hyphal morphogenesis, biofilm formation, and virulence of Candida albicans","volume":"114","author":"Graham","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1871","DOI":"10.1016\/j.peptides.2008.07.005","article-title":"First isolation of a novel thermostable antifungal peptide secreted by Aspergillus clavatus","volume":"29","author":"Gargouri","year":"2008","journal-title":"Peptides"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.4014\/jmb.1405.05008","article-title":"Purification and identification of a novel antifungal protein secreted by Penicillium citrinum from the Southwest Indian Ocean","volume":"24","author":"Wen","year":"2014","journal-title":"J. Microbiol. Biotechnol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.7164\/antibiotics.46.1414","article-title":"Biological properties of aureobasidin A, a cyclic depsipeptide antifungal antibiotic","volume":"46","author":"Takesako","year":"1993","journal-title":"J. Antibiot."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"919","DOI":"10.7164\/antibiotics.44.919","article-title":"Aureobasidins, new antifungal antibiotics. Taxonomy, fermentation, isolation, and properties","volume":"44","author":"Takesako","year":"1991","journal-title":"J. Antibiot."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1038\/ja.2016.107","article-title":"ASP2397: A novel antifungal agent produced by Acremonium persicinum MF-347833","volume":"70","author":"Nakamura","year":"2017","journal-title":"J. Antibiot."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1007\/s10126-008-9126-5","article-title":"Characterization of antifungal chitinase from marine Streptomyces sp. DA11 associated with South China Sea sponge Craniella australiensis","volume":"11","author":"Han","year":"2009","journal-title":"Mar. Biotechnol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"622","DOI":"10.7164\/antibiotics.56.622","article-title":"Chandrananimycins A approximately C: Production of novel anticancer antibiotics from a marine Actinomadura sp. isolate M048 by variation of medium composition and growth conditions","volume":"56","author":"Maskey","year":"2003","journal-title":"J. Antibiot."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1128\/AAC.23.6.926","article-title":"Polyoxin D inhibits growth of zoopathogenic fungi","volume":"23","author":"Becker","year":"1983","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1128\/AAC.34.4.587","article-title":"Evaluation of nikkomycins X and Z in murine models of coccidioidomycosis, histoplasmosis, and blastomycosis","volume":"34","author":"Hector","year":"1990","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_49","first-page":"961","article-title":"In-vitro activity of nikkomycin Z alone and in combination with polyenes, triazoles or echinocandins against Aspergillus fumigatus","volume":"10","author":"Ganesan","year":"2004","journal-title":"Clin. Microbiol. Infect. Off. Publ. Eur. Soc. Clin. Microbiol. Infect. Dis."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.pestbp.2019.09.003","article-title":"Antifungal activity of endophytic Bacillus safensis B21 and its potential application as a biopesticide to control rice blast","volume":"162","author":"Rong","year":"2020","journal-title":"Pestic. Biochem. Physiol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1111\/cbdd.13500","article-title":"Isolation, functional characterization, and biological properties of MCh-AMP1, a novel antifungal peptide from Matricaria chamomilla L.","volume":"93","author":"Seyedjavadi","year":"2019","journal-title":"Chem. Biol. Drug Des."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"25000","DOI":"10.1007\/s11356-017-0179-8","article-title":"Isolation and identification of antifungal peptides from Bacillus amyloliquefaciens W10","volume":"24","author":"Zhang","year":"2017","journal-title":"Environ. Sci. Pollut. Res. Int."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s11274-016-2024-5","article-title":"Purification and characterization of a potential antifungal protein from Bacillus subtilis E1R-J against Valsa mali","volume":"32","author":"Wang","year":"2016","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/j.biortech.2009.07.071","article-title":"Study of the antifungal activity of Bacillus vallismortis ZZ185 in vitro and identification of its antifungal components","volume":"101","author":"Zhao","year":"2010","journal-title":"Bioresour. Technol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"968487","DOI":"10.1155\/2014\/968487","article-title":"A broad-spectrum antimicrobial activity of Bacillus subtilis RLID 12.1","volume":"2014","author":"Ramachandran","year":"2014","journal-title":"Sci. World J."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1623","DOI":"10.1007\/s11274-011-0968-z","article-title":"A surfactant tolerant laccase of Meripilus giganteus","volume":"28","author":"Schmidt","year":"2012","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.jmii.2013.05.004","article-title":"Antimicrobial activity of a UV-stable bacteriocin-like inhibitory substance (BLIS) produced by Enterococcus faecium strain DSH20 against vancomycin-resistant Enterococcus (VRE) strains","volume":"47","author":"Shokri","year":"2014","journal-title":"J. Microbiol. Immunol. Infect. Wei Mian Yu Gan Ran Za Zhi"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1007\/s00284-005-0004-3","article-title":"Purification and characterization of two novel antimicrobial peptides Subpeptin JM4-A and Subpeptin JM4-B produced by Bacillus subtilis JM4","volume":"51","author":"Wu","year":"2005","journal-title":"Curr. Microbiol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1016\/j.fm.2019.03.021","article-title":"Isolation and characterisation of the antifungal activity of the cowpea defensin Cp-thionin II","volume":"82","author":"Schmidt","year":"2019","journal-title":"Food Microbiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1080\/14787210.2016.1199272","article-title":"Antifungal agents and liver toxicity: A complex interaction","volume":"14","author":"Tverdek","year":"2016","journal-title":"Expert Rev. Anti-Infect. Ther."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1007\/s40265-013-0069-4","article-title":"Amphotericin B formulations: A comparative review of efficacy and toxicity","volume":"73","author":"Hamill","year":"2013","journal-title":"Drugs"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1358\/dot.2002.38.12.820101","article-title":"Caspofungin","volume":"38","author":"Chandrasekar","year":"2002","journal-title":"Drugs Today"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1016\/S0140-6736(03)14472-8","article-title":"Echinocandin antifungal drugs","volume":"362","author":"Denning","year":"2003","journal-title":"Lancet"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1517\/13543776.2011.603899","article-title":"New \u03b2-glucan inhibitors as antifungal drugs","volume":"21","author":"Hector","year":"2011","journal-title":"Expert Opin. Ther. Pat."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1146\/annurev.mi.48.100194.002351","article-title":"Antibiotics that inhibit fungal cell wall development","volume":"48","author":"Debono","year":"1994","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.bbamem.2005.05.003","article-title":"Further aspects on the hemolytic activity of the antibiotic lipopeptide iturin A","volume":"1713","author":"Aranda","year":"2005","journal-title":"Biochim. Et Biophys. Acta"},{"key":"ref_67","first-page":"3315","article-title":"Cm-p5: An antifungal hydrophilic peptide derived from the coastal mollusk Cenchritis muricatus (Gastropoda: Littorinidae)","volume":"29","author":"McBeth","year":"2015","journal-title":"FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.bbamem.2007.09.020","article-title":"Amphipathic alpha-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: Pore formation mechanism in various lipid compositions","volume":"1778","author":"Park","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0925-4439(99)00097-6","article-title":"Inositol phosphoryl transferases from human pathogenic fungi","volume":"1500","author":"Heidler","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1002\/em.20656","article-title":"Characterization of environmental chemicals with potential for DNA damage using isogenic DNA repair-deficient chicken DT40 cell lines","volume":"52","author":"Yamamoto","year":"2011","journal-title":"Environ. Mol. Mutagenesis"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1080\/14786419.2018.1431630","article-title":"Antifungal effects of actinomycin D on Verticillium dahliae via a membrane-splitting mechanism","volume":"33","author":"Zeng","year":"2019","journal-title":"Nat. Prod. Res."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1042\/CBI20100035","article-title":"Inhibition of microRNA-14 contributes to actinomycin-D-induced apoptosis in the Sf9 insect cell line","volume":"34","author":"Kumarswamy","year":"2010","journal-title":"Cell Biol. Int."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1111\/j.1749-6632.1988.tb40398.x","article-title":"Synthesis and evaluation of LY121019, a member of a series of semisynthetic analogues of the antifungal lipopeptide echinocandin B","volume":"544","author":"Debono","year":"1988","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.addr.2012.09.037","article-title":"Liposomal drug delivery systems: From concept to clinical applications","volume":"65","author":"Allen","year":"2013","journal-title":"Adv. Drug Deliv. Rev."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1128\/CMR.00056-05","article-title":"Peptide antimicrobial agents","volume":"19","author":"Jenssen","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_76","first-page":"2993","article-title":"The Fungal Cell Wall: Candida, Cryptococcus, and Aspergillus Species","volume":"10","author":"Rivera","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"597","DOI":"10.3390\/medicina43080076","article-title":"Effects of beta-glucans on the immune system","volume":"43","author":"Akramiene","year":"2007","journal-title":"Medicina"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1007\/s40262-017-0578-5","article-title":"Clinical Pharmacokinetics and Pharmacodynamics of Micafungin","volume":"57","author":"Wasmann","year":"2018","journal-title":"Clin. Pharm."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"9881","DOI":"10.1007\/s00253-018-9382-x","article-title":"Biosynthesis of pneumocandin lipopeptides and perspectives for its production and related echinocandins","volume":"102","author":"Li","year":"2018","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1002\/ps.363","article-title":"Chitin synthesis and inhibition: A revisit","volume":"57","author":"Cohen","year":"2001","journal-title":"Pest. Manag. Sci."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1016\/j.mib.2010.05.002","article-title":"Chitin synthesis and fungal pathogenesis","volume":"13","author":"Lenardon","year":"2010","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1128\/AAC.01486-12","article-title":"Elevated chitin content reduces the susceptibility of Candida species to caspofungin","volume":"57","author":"Walker","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"227","DOI":"10.2174\/1389203720666190906165111","article-title":"Breakpoint: Cell Wall and Glycoproteins and their Crucial Role in the Phytopathogenic Fungi Infection","volume":"21","author":"Plaza","year":"2020","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"5300","DOI":"10.1016\/j.bmc.2011.08.010","article-title":"Antifungal thiopeptide cyclothiazomycin B1 exhibits growth inhibition accompanying morphological changes via binding to fungal cell wall chitin","volume":"19","author":"Mizuhara","year":"2011","journal-title":"Bioorganic Med. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Larwood, D.J. (2020). Nikkomycin Z-Ready to Meet the Promise?. J. Fungi, 6.","DOI":"10.3390\/jof6040261"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"73","DOI":"10.2174\/1381612805666230109204948","article-title":"Polyoxins and nikkomycins: Progress in synthetic and biological studies","volume":"5","author":"Zhang","year":"1999","journal-title":"Curr. Pharm. Des."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"2894","DOI":"10.1128\/AAC.02647-13","article-title":"Modulation of Alternaria infectoria cell wall chitin and glucan synthesis by cell wall synthase inhibitors","volume":"58","author":"Fernandes","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"5932","DOI":"10.1128\/AAC.00862-15","article-title":"Caspofungin Treatment of Aspergillus fumigatus Results in ChsG-Dependent Upregulation of Chitin Synthesis and the Formation of Chitin-Rich Microcolonies","volume":"59","author":"Walker","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1111\/mpp.12070","article-title":"Both extracellular chitinase and a new cyclic lipopeptide, chromobactomycin, contribute to the biocontrol activity of Chromobacterium sp. C61","volume":"15","author":"Kim","year":"2014","journal-title":"Mol. Plant Pathol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1080\/02681219780000971","article-title":"Molecular bases of adhesion of Candida albicans","volume":"35","author":"Fukazawa","year":"1997","journal-title":"J. Med. Vet. Mycol."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Hall, R.A., Bates, S., Lenardon, M.D., Maccallum, D.M., Wagener, J., Lowman, D.W., Kruppa, M.D., Williams, D.L., Odds, F.C., and Brown, A.J. (2013). The Mnn2 mannosyltransferase family modulates mannoprotein fibril length, immune recognition and virulence of Candida albicans. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003276"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1007\/BF01575126","article-title":"Pradimicins: A novel class of broad-spectrum antifungal compounds","volume":"16","author":"Walsh","year":"1997","journal-title":"Eur. J. Clin. Microbiol. Infect. Dis."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"768","DOI":"10.7164\/antibiotics.56.768","article-title":"Apoptosis-like cell death of Saccharomyces cerevisiae induced by a mannose-binding antifungal antibiotic, pradimicin","volume":"56","author":"Hiramoto","year":"2003","journal-title":"J. Antibiot."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1271\/bbb.69.238","article-title":"Pradimicin resistance of yeast is caused by a mutation of the putative N-glycosylation sites of osmosensor protein Sln1","volume":"69","author":"Hiramoto","year":"2005","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1128\/AAC.39.3.720","article-title":"Successful treatment of Pneumocystis carinii Pneumonia in mice with benanomicin A (ME1451)","volume":"39","author":"Yasuoka","year":"1995","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.toxicon.2020.03.011","article-title":"Use of Lactobacillus paracasei strain for zearalenone binding and metabolization","volume":"181","author":"Rogowska","year":"2020","journal-title":"Toxicon Off. J. Int. Soc. Toxinology"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1038","DOI":"10.1111\/j.1365-2672.2004.02385.x","article-title":"Ochratoxin A removal in synthetic and natural grape juices by selected oenological Saccharomyces strains","volume":"97","author":"Bejaoui","year":"2004","journal-title":"J. Appl. Microbiol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"4957","DOI":"10.1128\/AAC.49.12.4957-4964.2005","article-title":"Antimicrobial activities and structures of two linear cationic peptide families with various amphipathic beta-sheet and alpha-helical potentials","volume":"49","author":"Jin","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"27899","DOI":"10.1074\/jbc.M102865200","article-title":"A novel linear amphipathic beta-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids","volume":"276","author":"Blazyk","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1021\/bi0514515","article-title":"Lytic activity and structural differences of amphipathic peptides derived from trialysin","volume":"45","author":"Martins","year":"2006","journal-title":"Biochemistry"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1111\/j.1432-1033.1994.01019.x","article-title":"Secondary structure and membrane interaction of PR-39, a Pro+Arg-rich antibacterial peptide","volume":"224","author":"Cabiaux","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.jaad.2004.08.026","article-title":"Antimicrobial peptides","volume":"52","author":"Izadpanah","year":"2005","journal-title":"J. Am. Acad. Dermatol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.3390\/ph6081055","article-title":"Characterization of Antimicrobial Peptides toward the Development of Novel Antibiotics","volume":"6","author":"Aoki","year":"2013","journal-title":"Pharmaceuticals"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"72","DOI":"10.2174\/2211550111201010072","article-title":"Post-translational Modifications of Natural Antimicrobial Peptides and Strategies for Peptide Engineering","volume":"1","author":"Wang","year":"2012","journal-title":"Curr. Biotechnol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"3590","DOI":"10.1021\/bi036153r","article-title":"Energetics of pore formation induced by membrane active peptides","volume":"43","author":"Lee","year":"2004","journal-title":"Biochemistry"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"759","DOI":"10.4014\/jmb.1411.11058","article-title":"Antimicrobial Peptides (AMPs) with Dual Mechanisms: Membrane Disruption and Apoptosis","volume":"25","author":"Lee","year":"2015","journal-title":"J. Microbiol. Biotechnol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1007\/978-981-13-3588-4_2","article-title":"Membrane Permeabilization Mechanisms","volume":"1117","author":"Matsuzaki","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"2282","DOI":"10.1021\/acs.biochem.9b00180","article-title":"The Perpendicular Orientation of Amphotericin B Methyl Ester in Hydrated Lipid Bilayers Supports the Barrel-Stave Model","volume":"58","author":"Yamamoto","year":"2019","journal-title":"Biochemistry"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"11855","DOI":"10.1021\/ja9033473","article-title":"Direct interaction between amphotericin B and ergosterol in lipid bilayers as revealed by 2H NMR spectroscopy","volume":"131","author":"Matsumori","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"6627","DOI":"10.1128\/AAC.03570-14","article-title":"The production of reactive oxygen species is a universal action mechanism of Amphotericin B against pathogenic yeasts and contributes to the fungicidal effect of this drug","volume":"58","author":"Casas","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"16743","DOI":"10.1021\/jp061916g","article-title":"Modulation of amphotericin B membrane interaction by cholesterol and ergosterol---A molecular dynamics study","volume":"110","author":"Czub","year":"2006","journal-title":"J. Phys. Chem. B"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"106317","DOI":"10.1016\/j.bpc.2019.106317","article-title":"Interaction of amphotericin B and saturated or unsaturated phospholipid monolayers containing cholesterol or ergosterol at the air-water interface","volume":"258","author":"Wang","year":"2020","journal-title":"Biophys. Chem."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1021\/bi2012542","article-title":"Head-to-tail interaction between amphotericin B and ergosterol occurs in hydrated phospholipid membrane","volume":"51","author":"Umegawa","year":"2012","journal-title":"Biochemistry"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"2553","DOI":"10.1128\/AAC.06098-11","article-title":"Dynamic interaction between fluconazole and amphotericin B against Cryptococcus gattii","volume":"56","author":"Santos","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1007\/s00726-017-2441-2","article-title":"Glycotriazole-peptides derived from the peptide HSP1: Synergistic effect of triazole and saccharide rings on the antifungal activity","volume":"49","author":"Junior","year":"2017","journal-title":"Amino Acids"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0005-2736(99)00200-X","article-title":"Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides","volume":"1462","author":"Shai","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1094\/MPMI-8-0610","article-title":"Role of biosurfactant and ion channel-forming activities of syringomycin in transmembrane ion flux: A model for the mechanism of action in the plant-pathogen interaction","volume":"8","author":"Hutchison","year":"1995","journal-title":"Mol. Plant-Microbe Interact. MPMI"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"11279","DOI":"10.1021\/bi050898a","article-title":"Isothermal titration calorimetry studies of the binding of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes","volume":"44","author":"Abraham","year":"2005","journal-title":"Biochemistry"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.peptides.2007.10.028","article-title":"Effect of cholesterol on the interaction of the amphibian antimicrobial peptide DD K with liposomes","volume":"29","author":"Verly","year":"2008","journal-title":"Peptides"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1016\/j.bbapap.2015.03.003","article-title":"The natural, peptaibolic peptide SPF-5506-A4 adopts a \u03b2-bend spiral structure, shows low hemolytic activity and targets membranes through formation of large pores","volume":"1854","author":"Christoffersen","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1016\/S0006-3495(01)75802-X","article-title":"Barrel-stave model or toroidal model? A case study on melittin pores","volume":"81","author":"Yang","year":"2001","journal-title":"Biophys. J."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S0005-2736(97)00051-5","article-title":"Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria","volume":"1327","author":"Matsuzaki","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/0300-483X(94)90159-7","article-title":"Iturins, a special class of pore-forming lipopeptides: Biological and physicochemical properties","volume":"87","author":"Peypoux","year":"1994","journal-title":"Toxicology"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/bs.ircmb.2020.02.004","article-title":"On the role of sphingolipids in cell survival and death","volume":"351","author":"Iessi","year":"2020","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"311","DOI":"10.2174\/1568005043340597","article-title":"IPC synthase as a useful target for antifungal drugs","volume":"4","author":"Sugimoto","year":"2004","journal-title":"Curr. Drug Targets. Infect. Disord."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"9809","DOI":"10.1074\/jbc.272.15.9809","article-title":"Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene","volume":"272","author":"Nagiec","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_127","first-page":"712","article-title":"Micafungin alters the amino acid, nucleic acid and central carbon metabolism of Candida albicans at subinhibitory concentrations: Novel insights into mechanisms of action","volume":"72","author":"Katragkou","year":"2017","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.chembiol.2018.11.002","article-title":"14-Helical \u03b2-Peptides Elicit Toxicity against C. albicans by Forming Pores in the Cell Membrane and Subsequently Disrupting Intracellular Organelles","volume":"26","author":"Lee","year":"2019","journal-title":"Cell Chem. Biol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.fgb.2017.05.002","article-title":"Mechanism of action of AMP-jsa9, a LI-F-type antimicrobial peptide produced by Paenibacillus polymyxa JSa-9, against Fusarium moniliforme","volume":"104","author":"Han","year":"2017","journal-title":"Fungal Genet. Biol. FG B"},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Dietl, A.M., Misslinger, M., Aguiar, M.M., Ivashov, V., Teis, D., Pfister, J., Decristoforo, C., Hermann, M., Sullivan, S.M., and Smith, L.R. (2019). The Siderophore Transporter Sit1 Determines Susceptibility to the Antifungal VL-2397. Antimicrob. Agents Chemother., 63.","DOI":"10.1128\/AAC.00807-19"},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Nakamura, I., Ohsumi, K., Takeda, S., Katsumata, K., Matsumoto, S., Akamatsu, S., Mitori, H., and Nakai, T. (2019). ASP2397 Is a Novel Natural Compound That Exhibits Rapid and Potent Fungicidal Activity against Aspergillus Species through a Specific Transporter. Antimicrob. Agents Chemother., 63.","DOI":"10.1128\/AAC.02689-18"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.jbiotec.2018.07.044","article-title":"Biological control of plant pathogens by Bacillus species","volume":"285","author":"Fira","year":"2018","journal-title":"J. Biotechnol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1128\/AEM.02645-12","article-title":"Contribution of bacillomycin D in Bacillus amyloliquefaciens SQR9 to antifungal activity and biofilm formation","volume":"79","author":"Xu","year":"2013","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1615\/CritRevImmunol.v20.i5.40","article-title":"Cationic antimicrobial peptides and their multifunctional role in the immune system","volume":"20","author":"Scott","year":"2000","journal-title":"Crit. Rev. Immunol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1038\/ncomms1046","article-title":"Mechanisms underlying beneficial plant-fungus interactions in mycorrhizal symbiosis","volume":"1","author":"Bonfante","year":"2010","journal-title":"Nat. Commun."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.3389\/fmicb.2019.01030","article-title":"Trichoderma as a Model to Study Effector-Like Molecules","volume":"10","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"2835","DOI":"10.1002\/ptr.6728","article-title":"Beneficial effects of Trichoderma secondary metabolites on crops","volume":"34","author":"Vinale","year":"2020","journal-title":"Phytother. Res. PTR"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Marra, R., Coppola, M., Pironti, A., Grasso, F., Lombardi, N., d\u2019Errico, G., Sicari, A., Bolletti Censi, S., Woo, S.L., and Rao, R. (2020). The Application of Trichoderma Strains or Metabolites Alters the Olive Leaf Metabolome and the Expression of Defense-Related Genes. J. Fungi, 6.","DOI":"10.3390\/jof6040369"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1046\/j.1462-2920.1999.00054.x","article-title":"Tomato seed and root exudate sugars: Composition, utilization by Pseudomonas biocontrol strains and role in rhizosphere colonization","volume":"1","author":"Lugtenberg","year":"1999","journal-title":"Environ. Microbiol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"103375","DOI":"10.1016\/j.fm.2019.103375","article-title":"Biocontrol ability and action mechanism of Metschnikowia citriensis against Geotrichum citri-aurantii causing sour rot of postharvest citrus fruit","volume":"87","author":"Wang","year":"2020","journal-title":"Food Microbiol."},{"key":"ref_141","first-page":"30","article-title":"Biological control of postharvest sour rot of citrus by two antagonistic yeasts","volume":"51","author":"Liu","year":"2010","journal-title":"Lett. Appl. Microbiol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1111\/1462-2920.12538","article-title":"The bacterial lipopeptide iturins induce Verticillium dahliae cell death by affecting fungal signalling pathways and mediate plant defence responses involved in pathogen-associated molecular pattern-triggered immunity","volume":"17","author":"Han","year":"2015","journal-title":"Environ. Microbiol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1007\/s12275-014-3605-3","article-title":"Effects of fengycin from Bacillus subtilis fmbJ on apoptosis and necrosis in Rhizopus stolonifer","volume":"52","author":"Tang","year":"2014","journal-title":"J. Microbiol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"8963","DOI":"10.1007\/s00253-019-10117-5","article-title":"C16-Fengycin A affect the growth of Candida albicans by destroying its cell wall and accumulating reactive oxygen species","volume":"103","author":"Liu","year":"2019","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Jiang, J., Gao, L., Bie, X., Lu, Z., Liu, H., Zhang, C., Lu, F., and Zhao, H. (2016). Identification of novel surfactin derivatives from NRPS modification of Bacillus subtilis and its antifungal activity against Fusarium moniliforme. BMC Microbiol., 16.","DOI":"10.1186\/s12866-016-0645-3"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1007\/s12275-011-0171-9","article-title":"Antifungal activity and mechanism of fengycin in the presence and absence of commercial surfactin against Rhizopus stolonifer","volume":"49","author":"Tao","year":"2011","journal-title":"J. Microbiol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"28831","DOI":"10.1074\/jbc.M303300200","article-title":"Antifungal activity of amiodarone is mediated by disruption of calcium homeostasis","volume":"278","author":"Gupta","year":"2003","journal-title":"J. Biol. Chem."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/11\/3438\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:11:17Z","timestamp":1760163077000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/11\/3438"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,6,5]]},"references-count":147,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2021,6]]}},"alternative-id":["molecules26113438"],"URL":"https:\/\/doi.org\/10.3390\/molecules26113438","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,6,5]]}}}