Abstract
Candida albicans, an opportunistic yeast pathogen, is equipped with a plethora of virulence attributes such as yeast-to-hyphae transition, secreted enzymes, tissue adhesion, and biofilm production. The dearth of effective anti-mycotics together with the emergence of drug-resistant C. albicans isolates underscore the need to explore novel anti-fungal agents. Anti-microbial peptides (AMPs) have recently awakened considerable interest as potential therapeutic agents. The intent of this study is to assess anti-fungal effects of Mastoparan VT-1 (MP-VT1), an AMP from the venom of social wasp Vespa tropica, against planktonic and biofilm-embedded cells of C. albicans. MP-VT1 had a tendency to adopt alpha-helical conformation based on peptide secondary structure prediction and circular dichroism spectroscopy (in 50% trifluoroethanol). The peptide showed MIC values ranging from 2 to 32 µg/mL against 10 clinical strains of C. albicans. Notably, a 6-h of exposure to 1 × MFC of MP-VT1 sufficed for total yeast clearance. At fungicidal concentrations, MP-VT1 exhibited slight cytotoxicity towards human dermal fibroblasts. Flow cytometric analysis and fluorescence microscopy revealed that MP-VT1 induced membrane disruption, leading to death of C. albicans mainly by necrosis. Interestingly, a significant inhibition of hyphal transition was noticed at 3 and 6 h post-contact with 32 µg/mL of MP-VT1. At sub-lethal concentrations, the peptide lessened not only candidal cell surface hydrophobicity but also the number of yeasts adhering to the polystyrene surfaces. Furthermore, C. albicans cells within biofilms were more vulnerable to MP-VT1 than to fluconazole. Overall, MP-VT1 has the potential to be used as a candidate for anti-fungal drug development.
Similar content being viewed by others
Abbreviations
- AMPs:
-
Anti-microbial peptides
- AO/EtBr:
-
Acridine orange/ethidium bromide
- CD:
-
Circular dichroism
- CFUs:
-
Colony forming units
- CSH:
-
Cell surface hydrophobicity
- DMEM:
-
Dulbecco’s Modifed Eagle’s Medium
- DMSO:
-
Dimethyl sulfoxide
- FCS:
-
Fetal calf serum
- FITC:
-
Fluorescein isothiocyanate
- HFFs:
-
Human foreskin fibroblasts
- MFC:
-
Minimum fungicidal concentration
- MIC:
-
Minimum inhibitory concentration
- MP-VT1:
-
Mastoparan VT-1
- MOPS:
-
3-(N-Morpholino) propane sulfonic acid
- OD:
-
Optical density
- PBS:
-
Phosphate-buffered saline
- PI:
-
Propidium iodide
- RP-HPLC:
-
Reversed phase–high-performance liquid chromatography
- RPMI 1640:
-
Roswell Park Memorial Institute 1640
- SD:
-
Standard deviation
- SDA:
-
Sabouraud dextrose agar
- SDB:
-
Sabouraud dextrose broth
- TFE:
-
2,2,2-Trifluoroethanol
- YNBG:
-
Yeast nitrogen base medium containing 2% glucose
References
Acar T, Pelit Arayıcı P, Ucar B, Karahan M, Mustafaeva Z (2019) Synthesis, characterization and lipophilicity study of Brucella abortus’ immunogenic peptide sequence that can be used in the future vaccination studies. Int J Pept Res Ther 25(3):911–918. https://doi.org/10.1007/s10989-018-9739-0
Adade CM, Oliveira IRS, Pais JAR, Souto-Padrón T (2013) Melittin peptide kills Trypanosoma cruzi parasites by inducing diferent cell death pathways. Toxicon 69:227–239. https://doi.org/10.1016/j.toxicon.2013.03.011
Adamczak R, Porollo A, Meller J (2005) Combining prediction of secondary structure and solvent accessibility in proteins. Proteins Struct Funct Bioinf 59(3):467–475. https://doi.org/10.1002/prot.20441
Andrä J, Berninghausen O, Leippe M (2001) Cecropins, antibacterial peptides from insects and mammals, are potently fungicidal against Candida albicans. Med Microbiol Immunol 189(3):169–173. https://doi.org/10.1007/s430-001-8025-x
Andrä J, Leippe M (1999) Candidacidal activity of shortened synthetic analogs of amoebapores and NK-lysin. Med Microbiol Immunol 188(3):117–124. https://doi.org/10.1007/s004300050113
Awouafack MD, McGaw LJ, Gottfried S, Mbouangouere R, Tane P, Spiteller M, Eloff JN (2013) Antimicrobial activity and cytotoxicity of the ethanol extract, fractions and eight compounds isolated from Eriosema robustum (Fabaceae). BMC Complement Altern Med 13:289. https://doi.org/10.1186/1472-6882-13-289
Batoni G, Maisetta G, Brancatisano FL, Esin S, Campa M (2011) Use of antimicrobial peptides against microbial biofilms: advantages and limits. Curr Med Chem 18(2):256–279. https://doi.org/10.2174/092986711794088399
Brauner A, Alvendal C, Chromek M, Stopsack KH, Ehrstrom S, Schroder JM, Bohm-Starke N (2018) Psoriasin, a novel anti-Candida albicans adhesin. J Mol Med (berl) 96(6):537–545. https://doi.org/10.1007/s00109-018-1637-6
Chang HT, Tsai PW, Huang HH, Liu YS, Chien TS, Lan CY (2012) LL37 and hBD-3 elevate the beta-1,3-exoglucanase activity of Candida albicans Xog1p, resulting in reduced fungal adhesion to plastic. Biochem J 441(3):963–970. https://doi.org/10.1042/BJ20111454
Chen X, Zhang L, Wu Y, Wang L, Ma C, Xi X, Bininda-Emonds ORP, Shaw C, Chen T, Zhou M (2018) Evaluation of the bioactivity of a mastoparan peptide from wasp venom and of its analogues designed through targeted engineering. Int J Biol Sci 14(6):599–607. https://doi.org/10.7150/ijbs.23419
Cho J, Lee DG (2011) Oxidative stress by antimicrobial peptide pleurocidin triggers apoptosis in Candida albicans. Biochimie 93(10):1873–1879. https://doi.org/10.1016/j.biochi.2011.07.011
Choi H, Lee DG (2014) Antifungal activity and pore-forming mechanism of astacidin 1 against Candida albicans. Biochimie 105:58–63. https://doi.org/10.1016/j.biochi.2014.06.014
CLSI, 2017. Reference method for broth dilution antifungal susceptibility testing of yeast, 4th edition: M27, Clinical and Laboratory Standards Institute, Wayne.
Culik RM, Abaskharon RM, Pazos IM, Gai F (2014) Experimental validation of the role of trifluoroethanol as a nanocrowder. J Phys Chem B 118(39):11455–11461. https://doi.org/10.1021/jp508056w
da Silva AV, De Souza BM, Dos Santos Cabrera MP, Dias NB, Gomes PC, Neto JR, Stabeli RG, Palma MS (2014) The effects of the C-terminal amidation of mastoparans on their biological actions and interactions with membrane-mimetic systems. Biochim Biophys Acta 1838:2357–2368. https://doi.org/10.1016/j.bbamem.2014.06.012
da Silva AM, Silva-Gonçalves LC, Oliveira FA, Arcisio-Miranda M (2018) Pro-necrotic activity of cationic mastoparan peptides in human glioblastoma multiforme cells via membranolytic action. Mol Neurobiol 55(7):5490–5504. https://doi.org/10.1007/s12035-017-0782-1
Danchik C, Casadevall A (2021) Role of cell surface hydrophobicity in the pathogenesis of medically-significant fungi. Front Cell Infect Microbiol 10:594973. https://doi.org/10.3389/fcimb.2020.594973
de Lacorte Singulani J, Galeane MC, Ramos MD, Gomes PC, Dos Santos CT, de Souza BM, Palma MS, Fusco Almeida AM, Mendes Giannini MJS (2019) Antifungal activity, toxicity, and membranolytic action of a mastoparan analog peptide. Front Cell Infect Microbiol 9:419. https://doi.org/10.3389/fcimb.2019.00419
de Souza BM, da Silva AV, Resende VM, Arcuri HA, dos Santos Cabrera MP, Neto JR, Palma MS (2009) Characterization of two novel polyfunctional mastoparan peptides from the venom of the social wasp Polybia paulista. Peptides 30(8):1387–1395. https://doi.org/10.1016/j.peptides.2009.05.008
Do N, Weindl G, Grohmann L, Salwiczek M, Koksch B, Korting HC, Schäfer-Korting M (2014) Cationic membrane-active peptides - anticancer and antifungal activity as well as penetration into human skin. Exp Dermatol 23(5):326–331. https://doi.org/10.1111/exd.12384
do Nascimento Dias J, de Souza Silva C, de Araujo AR, Souza JMT, de Holanda Veloso Junior PH, Cabral WF, da Gloria da Silva M, Eaton P, de Souza de Almeida Leite JR, Nicola AM, Albuquerque P, Silva-Pereira I (2020) Mechanisms of action of antimicrobial peptides ToAP2 and NDBP-5.7 against Candida albicans planktonic and biofilm cells. Sci Rep 10(1):10327. https://doi.org/10.1038/s41598-020-67041-2
Dudiuk C, Berrio I, Leonardelli F, Morales-Lopez S, Theill L, Macedo D, Yesid-Rodriguez J, Salcedo S, Marin A, Gamarra S, Garcia-Effron G (2019) Antifungal activity and killing kinetics of anidulafungin, caspofungin and amphotericin B against Candida auris. J Antimicrob Chemother 74(8):2295–2302. https://doi.org/10.1093/jac/dkz178
Ellepola AN, Joseph BK, Khan ZU (2013) Changes in the cell surface hydrophobicity of oral Candida albicans from smokers, diabetics, asthmatics, and healthy individuals following limited exposure to chlorhexidine gluconate. Med Princ Pract 22(3):250–254. https://doi.org/10.1159/000345641
El-Wahed AA, Yosri N, Sakr HH, Du M, Algethami AFM, Zhao C, Abdelazeem AH, Tahir HE, Masry SHD, Abdel-Daim MM, Musharraf SG, El-Garawani I, Kai G, Al Naggar Y, Khalifa SAM, El-Seedi HR (2021) Wasp venom biochemical components and their potential in biological applications and nanotechnological interventions. Toxins (Basel) 13(3):206. https://doi.org/10.3390/toxins13030206
Fazly A, Jain C, Dehner AC, Issi L, Lilly EA, Ali A, Cao H, Fidel PL Jr, Rao RP, Kaufman PD (2013) Chemical screening identifies filastatin, a small molecule inhibitor of Candida albicans adhesion, morphogenesis, and pathogenesis. Proc Natl Acad Sci USA 110(33):13594–13599. https://doi.org/10.1073/pnas.1305982110
Galeane MC, Gomes PC, Singulani JL, de Souza BM, Palma MS, Mendes-Giannini MJ, Almeida AM (2019) Study of mastoparan analog peptides against Candida albicans and safety in zebrafish embryos (Danio rerio). Future Microbiol 14:1087–1097. https://doi.org/10.2217/fmb-2019-0060
Goswami RR, Pohare SD, Raut JS, Karuppayil SM (2017) Cell surface hydrophobicity as a virulence factor in Candida albicans. Biosci Biotech Res Asia 14:1503–1511
Hazen KC, Hazen BW (1992) Hydrophobic surface protein masking by the opportunistic fungal pathogen Candida albicans. Infect Immun 60(4):1499–1508. https://doi.org/10.1128/iai.60.4.1499-1508.1992
Hilchie AL, Sharon AJ, Haney EF, Hoskin DW, Bally MB, Franco OL, Corcoran JA, Hancock RE (2016) Mastoparan is a membranolytic anti-cancer peptide that works synergistically with gemcitabine in a mouse model of mammary carcinoma. Biochim Biophys Acta 1858:3195–3204. https://doi.org/10.1016/j.bbamem.2016.09.021
Hossen S, Gan SH, Khalil I (2017) Melittin, a potential natural toxin of crude bee venom: probable future arsenal in the treatment of diabetes mellitus. J Chem 2017:1–7. https://doi.org/10.1155/2017/4035626
Indrayanto G, Putra GS, Suhud F (2021) Validation of in-vitro bioassay methods: application in herbal drug research. Profiles Drug Subst Excip Relat Methodol 46:273–307. https://doi.org/10.1016/bs.podrm.2020.07.005
Irazazabal LN, Porto WF, Ribeiro SM, Casale S, Humblot V, Ladram A, Franco OL (2016) Selective amino acid substitution reduces cytotoxicity of the antimicrobial peptide mastoparan. Biochim Biophys Acta 11:2699–2708. https://doi.org/10.1016/j.bbamem.2016.07.001
Kim Y, Son M, Noh EY, Kim S, Kim C, Yeo JH, Park C, Lee KW, Bang WY (2016) MP-V1 from the venom of social wasp Vespula vulgaris is a de novo type of mastoparan that displays superior antimicrobial activities. Molecules 21(4):512. https://doi.org/10.3390/molecules21040512
Kočendová J, Vaňková E, Volejníková A, Nešuta O, Buděšínský M, Socha O, Hájek M, Hadravová R, Čeřovský V (2019) Antifungal activity of analogues of antimicrobial peptides isolated from bee venoms against vulvovaginal Candida spp. FEMS Yeast Res 19(3):foz013. https://doi.org/10.1093/femsyr/foz013
Krausova G, Hyrslova I, Hynstova I (2019) In vitro evaluation of adhesion capacity, hydrophobicity, and auto-aggregation of newly isolated potential probiotic strains. Fermentation 5:100. https://doi.org/10.3390/fermentation5040100
Le Lay C, Akerey B, Fliss I, Subirade M, Rouabhia M (2008) Nisin Z inhibits the growth of Candida albicans and its transition from blastospore to hyphal form. J Appl Microbiol 105(5):1630–1639. https://doi.org/10.1111/j.1365-2672.2008.03908.x
Lee G, Bae H (2016) Anti-inflammatory applications of melittin, a major component of bee venom: detailed mechanism of action and adverse effects. Molecules. https://doi.org/10.3390/molecules21050616
Lee DL, Mant CT, Hodges RS (2003) A novel method to measure self-association of small amphipathic molecules: temperature profiling in reversed-phase chromatography. J Biol Chem 278(25):22918–22927. https://doi.org/10.1074/jbc.M301777200
Lee Y, Puumala E, Robbins N, Cowen LE (2021) Antifungal drug resistance: molecular mechanisms in Candida albicans and beyond. Chem Rev 121(6):3390–3411. https://doi.org/10.1021/acs.chemrev.0c00199
Lee H, Woo ER, Lee DG (2018) Apigenin induces cell shrinkage in Candida albicans by membrane perturbation. FEMS Yeast Res 18(1):foy003. https://doi.org/10.1093/femsyr/foy003
Lima WG, Batista Filho FL, Lima IP, Simião DC, Brito JCM, da CruzNizer WS, Cardoso VN, Fernandes SOA (2022) Antibacterial, anti-biofilm, and anti-adhesive activities of melittin, a honeybee venom-derived peptide, against quinolone-resistant uropathogenic Escherichia coli (UPEC) Nat Prod Res. https://doi.org/10.1080/14786419.2022.2032047
Lohse MB, Gulati M, Johnson AD, Nobile CJ (2018) Development and regulation of single and multi-species Candida albicans biofilms. Nat Rev Microbiol 16(1):19–31. https://doi.org/10.1038/nrmicro.2017.107
Lum KY, Tay ST, Le CF, Lee VS, Sabri NH, Velayuthan RD, Hassan H, Sekaran SD (2015) Activity of novel synthetic peptides against Candida albicans. Sci Rep 5:9657. https://doi.org/10.1038/srep09657
Lyu C, Fang F, Li B (2019) Anti-tumor effects of melittin and its potential applications in clinic. Curr Protein Pept Sci 20(3):240–250. https://doi.org/10.2174/1389203719666180612084615
Lyu Y, Yang Y, Lyu X, Dong N, Shan A (2016) Antimicrobial activity, improved cell selectivity and mode of action of short PMAP-36-derived peptides against bacteria and Candida. Sci Rep 6:27258. https://doi.org/10.1038/srep27258
Mayer FL, Wilson D, Hube B (2013) Candida albicans pathogenicity mechanisms. Virulence 4(2):119–128. https://doi.org/10.4161/viru.22913
Memariani H, Memariani M (2021) Melittin as a promising anti-protozoan peptide: current knowledge and future prospects. AMB Express 11(1):69. https://doi.org/10.1186/s13568-021-01229-1
Memariani H, Memariani M (2020) Anti-fungal properties and mechanisms of melittin. Appl Microbiol Biotechnol 104(15):6513–6526. https://doi.org/10.1007/s00253-020-10701-0
Memariani H, Memariani M, Robati RM, Nasiri S, Abdollahimajd F, Baseri Z, Moravvej H (2020) Anti-Staphylococcal and cytotoxic activities of the short anti-microbial peptide PVP. World J Microbiol Biotechnol 36(11):174. https://doi.org/10.1007/s11274-020-02948-6
Memariani H, Memariani M, Shahidi-Dadras M, Nasiri S, Akhavan MM, Moravvej H (2019) Melittin: from honeybees to superbugs. Appl Microbiol Biotechnol 103(8):3265–3276. https://doi.org/10.1007/s00253-019-09698-y
Memariani H, Shahbazzadeh D, Ranjbar R, Behdani M, Memariani M, Bagheri KP (2017) Design and characterization of short hybrid antimicrobial peptides from pEM-2, mastoparan-VT1, and mastoparan-B. Chem Biol Drug Des 89(3):327–338. https://doi.org/10.1111/cbdd.12864
Memariani H, Shahbazzadeh D, Sabatier JM, Pooshang Bagheri K (2018) Membrane-active peptide PV3 efficiently eradicates multidrug-resistant Pseudomonas aeruginosa in a mouse model of burn infection. APMIS 126(2):114–122. https://doi.org/10.1111/apm.12791
Mohamed MF, Abdelkhalek A, Seleem MN (2016) Evaluation of short synthetic antimicrobial peptides for treatment of drug-resistant and intracellular Staphylococcus aureus. Sci Rep 6:29707. https://doi.org/10.1038/srep29707
Moreno M, Giralt E (2015) Three valuable peptides from bee and wasp venoms for therapeutic and biotechnological use: melittin, apamin and mastoparan. Toxins (basel) 7(4):1126–1150. https://doi.org/10.3390/toxins7041126
Nobile CJ, Johnson AD (2015) Candida albicans biofilms and human disease. Annu Rev Microbiol 69:71–92. https://doi.org/10.1146/annurev-micro-091014-104330
Olsen I (2015) Biofilm-specific antibiotic tolerance and resistance. Eur J Clin Microbiol Infect Dis 34(5):877–886. https://doi.org/10.1007/s10096-015-2323-z
Park C, Lee DG (2009) Fungicidal effect of antimicrobial peptide arenicin-1. Biochim Biophys Acta 1788(9):1790–1796. https://doi.org/10.1016/j.bbamem.2009.06.008
Park SC, Kim JY, Kim EJ, Cheong GW, Lee Y, Choi W, Lee JR, Jang MK (2018) Hydrophilic linear peptide with histidine and lysine residues as a key factor affecting antifungal activity. Int J Mol Sci 19(12):3781. https://doi.org/10.3390/ijms19123781
Porto WF, Irazazabal L, Alves ESF, Ribeiro SM, Matos CO, Pires ÁS, Fensterseifer ICM, Miranda VJ, Haney EF, Humblot V, Torres MDT, Hancock REW, Liao LM, Ladram A, Lu TK, de la Fuente-Nunez S, Franco OC (2018) In silico optimization of a guava antimicrobial peptide enables combinatorial exploration for peptide design. Nat Commun 9(1):1490. https://doi.org/10.1038/s41467-018-03746-3
Raja Z, André S, Abbassi F, Humblot V, Lequin O, Bouceba T, Correia I, Casale S, Foulon T, Sereno D, Oury B, Ladram A (2017) Insight into the mechanism of action of temporin-SHa, a new broad-spectrum antiparasitic and antibacterial agent. PLoS ONE 12(3):e0174024. https://doi.org/10.1371/journal.pone.0174024
Reen FJ, Phelan JP, Gallagher L, Woods DF, Shanahan RM, Cano R, Eoin M, McGlacken GP, Oara F (2016) Exploiting interkingdom interactions for development of small-molecule inhibitors of Candida albicans biofilm formation. Antimicrob Agents Chemother 60(10):5894–5905. https://doi.org/10.1128/AAC.00190-16
Rončević T, Puizina J, Tossi A (2019) Antimicrobial peptides as anti-infective agents in pre-post-antibiotic era? Int J Mol Sci 20 (22). https://doi.org/10.3390/ijms20225713
Scarsini M, Tomasinsig L, Arzese A, D’Este F, Oro D, Skerlavaj B (2015) Antifungal activity of cathelicidin peptides against planktonic and biofilm cultures of Candida species isolated from vaginal infections. Peptides 71:211–221. https://doi.org/10.1016/j.peptides.2015.07.023
Silva ON, Torres MDT, Cao J, Alves ESF, Rodrigues LV, Resende JM, Liao LM, Porto WF, Fensterseifer ICM, Lu TK, Franco OL, de la Fuente-Nunez C (2020) Repurposing a peptide toxin from wasp venom into antiinfectives with dual antimicrobial and immunomodulatory properties. Proc Natl Acad Sci USA 117(43):26936–26945. https://doi.org/10.1073/pnas.2012379117
Singleton DR, Fidel PL Jr, Wozniak KL, Hazen KC (2005) Contribution of cell surface hydrophobicity protein 1 (Csh1p) to virulence of hydrophobic Candida albicans serotype A cells. FEMS Microbiol Lett 244(2):373–377. https://doi.org/10.1016/j.femsle.2005.02.010
Smart SS, Mason TJ, Bennell PS, Maeij NJ, Geysen HM (1996) High-throughput purity estimation and characterisation of synthetic peptides by electrospray mass spectrometry. Int J Pept Protein Res 47(1–2):47–55. https://doi.org/10.1111/j.1399-3011.1996.tb00809.x
Snyder SS, Gleaton JW, Kirui D, Chen W, Millenbaugh NJ (2021) Antifungal activity of synthetic scorpion venom-derived peptide analogues against Candida albicans. Int J Pept Res Ther 27:281–291. https://doi.org/10.1007/s10989-020-10084-w
Talapko J, Juzbasic M, Matijevic T, Pustijanac E, Bekic S, Kotris I, Skrlec I (2021) Candida albicans—the virulence factors and clinical manifestations of infection. J Fungi (Basel) 7(2):79. https://doi.org/10.3390/jof7020079
Tan L, Bai L, Wang L, He L, Li G, Du W, Shen T, Xiang Z, Wu J, Liu Z, Hu M (2018) Antifungal activity of spider venom-derived peptide lycosin-I against Candida tropicalis. Microbiol Res 216:120–128. https://doi.org/10.1016/j.micres.2018.08.012
Tsai PW, Yang CY, Chang HT, Lan CY (2011) Human antimicrobial peptide LL-37 inhibits adhesion of Candida albicans by interacting with yeast cell-wall carbohydrates. PLoS ONE 6(3):e17755. https://doi.org/10.1371/journal.pone.0017755
Tsang PW, Bandara HM, Fong WP (2012) Purpurin suppresses Candida albicans biofilm formation and hyphal development. PLoS ONE 7(11):e50866. https://doi.org/10.1371/journal.pone.0050866
Uddin MB, LeeBH NC, Kim JH, Kim TH, Lee HC, Kim CG, Lee JS, Kim CJ (2016) Inhibitory effects of bee venom and its components against viruses in vitro and in vivo. J Microbiol 54(12):853–866. https://doi.org/10.1007/s12275-016-6376-1
Vaňková E, Kašparová P, Dulíčková N, Čeřovský V (2020) Combined effect of lasioglossin LL-III derivative with azoles against Candida albicans virulence factors: biofilm formation, phospholipases, proteases and hemolytic activity. FEMS Yeast Res 20(3):foaa020. https://doi.org/10.1093/femsyr/foaa020
Vila-Farrés X, López-Rojas R, Pachón-Ibánez ME, Teixidó M, Pachón J, Vila J, Giralt E (2015) Sequence-activity relationship, and mechanism of action of mastoparan analogues against extended-drug resistant Acinetobacter baumannii. EurJ Med Chem 101:34–40. https://doi.org/10.1016/j.ejmech.2015.06.016
Vrablikova A, Czernekova L, Cahlikova R, Novy Z, Petrik M, Imran S, Novak Z, Krupka M, Cerovsky V, Turanek J, Raska M (2017) Lasioglossins LLIII affect the morphogenesis of Candida albicans and reduces the duration of experimental vaginal candidiasis in mice. Microbiol Immunol 61(11):474–481. https://doi.org/10.1111/1348-0421.12538
Walsh TJMD, Hayden RT, Larone DH (2018) Larone’s medically important fungi: a guide to identification, 6th edn. ASM Press, Washington, DC
Wang K, Yan J, Dang W, Xie J, Yan B, Yan W, Sun M, Zhang B, Ma M, Zhao Y, Jia F, Zhu R, Chen W, Wang R (2014) Dual antifungal properties of cationic antimicrobial peptides polybia-MPI: membrane integrity disruption and inhibition of biofilm formation. Peptides 56:22–29. https://doi.org/10.1016/j.peptides.2014.03.005
Yang X, Wang Y, Lee WH, Zhang Y (2013) Antimicrobial peptides from the venom gland of the social wasp Vespa tropica. Toxiconomy 74:151–157. https://doi.org/10.1016/j.toxicon.2013.08.056
Author information
Authors and Affiliations
Contributions
MM and HM jointly contributed to all phases of this study (conception, experimental design, data analysis, practical work, and authorship of the manuscript). ZP and ZB partially participated in practical work. HM critically reviewed and edited the manuscript. All authors read and approved the final manuscript.
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no competing interests.
Ethical Approval
The manuscript does not contain experiments involving animal or human studies.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Supplementary Information
Below is the link to the electronic supplementary material.
Fig. S1
RP-HPLC chromatogram (a) and mass spectrum (b) of synthetic mastoparan VT-1 (INLKAIAALAKKLL—NH2). In panel a, insert represents additional information on retention time (RT), peak area, peak height, and % area. As shown in panel a, the large peak assigned with the black arrow represents the purified peptide. (TIF 2647 KB)
Rights and permissions
About this article
Cite this article
Memariani, M., Memariani, H., Poursafavi, Z. et al. Anti-fungal Effects and Mechanisms of Action of Wasp Venom-Derived Peptide Mastoparan-VT1 Against Candida albicans. Int J Pept Res Ther 28, 96 (2022). https://doi.org/10.1007/s10989-022-10401-5
Accepted:
Published:
DOI: https://doi.org/10.1007/s10989-022-10401-5