Natural Antimicrobial Peptides as Inspiration for Design of a New Generation Antifungal Compounds
Abstract
:1. Introduction
2. Antifungal Peptides
2.1. Natural Peptides
2.1.1. Bacterial and Fungal Peptides
2.1.2. Plant Peptides
2.1.3. Insect Peptides
2.1.4. Amphibian Peptides
2.1.5. Avian and Mammalian Antifungal Peptides
2.2. Interactions of Natural Antifungal Peptides with Other Antifungal Drugs
2.3. Natural Antifungal Peptides in New Delivery Systems
2.4. Synthetic Peptides and Peptide Derivatives
2.5. Dendrimeric Peptide Mimics
2.5.1. Dendrimers as Carriers of Bioactive Substances and Solubility Enhancers
2.5.2. Inherent Activity of Dendrimeric Peptide Mimics and Their Antifungal Formulations
3. Conclusions
Acknowledgments
Authors contribution
Conflicts of Interest
References
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Risk Factors | References |
---|---|
Abdominal surgery/recent major surgery | [3,5,9,10] |
Deep burns | [11,12] |
Diabetes mellitus | [9,10,12] |
Dialysis | [12,13] |
Disturbance of natural skin or mucosal barriers | [10,12] |
Exposure to broad-spectrum antibiotics | [3,10,12] |
Extremes of age | [5,10] |
HIV/AIDS | [9,13] |
Immune disorders | [5,11] |
Local disorders of the gastrointestinal tract | [5,10,12] |
Long-term catheterization | [3,5,13] |
Malignancies | [3,5] |
Mechanical ventilation | [10,13] |
Parenteral nutrition | [5,10,13] |
Premature very low birth weight infants | [11] |
Prolonged hospitalization | [12] |
Renal failure | [9,11,12] |
Solid organ or bone marrow transplantation | [5] |
Treatment with corticosteroids | [3,5] |
Use of immunosuppressive drugs | [5,10,12] |
Group Name | Group Member/s | Mode of Action | Resistance Mechanism | References |
---|---|---|---|---|
Fluorinated Pyrimidine Analogs | Flucytosine (5-FC) | Inhibition of RNA and/or DNA synthesis |
| [15,52] |
Polyenes | Nystatin Natamycin Amphotericin B | Alteration of the membrane function by binding of ergosterol (depleting cells of ergosterol) |
| [18,52] |
Echinocandins | Caspofungin Micafungin Anidulafungin | Alteration of cell wall biosynthesis by inhibition of β(1,3)-glucan synthase Fks1p or Fks2p |
| [16,19] |
Allylamines | Terbinafine Naftifine | Inhibition of the ergosterol biosynthesis by inhibition of squalene epoxidase (Erg1) and/or accumulation of toxic sterol intermediates |
| [16,19] |
Azoles | Fluconazole Posoconazole Voriconazole | Inhibition of cytochrome P450 14α-lanosterol demethylase (encoded by ERG11) in ergosterol biosynthesis pathway |
| [16,19,52] |
Name | Origin | Sequence or Molecular Formula | Mode of Action | Reference |
---|---|---|---|---|
Bacterial Peptides | ||||
Syringomycin | Pseudomonas syringae pv. syringae | MSLQANTAPVFADEQQTDAPTWPDRAADPSVRLSLLATGNSLPVVIEPTADGLDPVQWASARREAIETLLCRHGAVLFRGFDLPSVAAFEGFAEALSPGLHGTYGDLPKKEGGRNVYRSTPYPEREMILYHNESSHLESWPRKQWFFCEQPSRVGGATPLADIRQVLAYLPKEVVERFESKGLLYSRTFTAGVEPSWESFFGTSERSVIEQRCREQGTDFEWLDGDTLQLRTQCPAVITHPFTGERCFFNQVQLHHPYCMGEELREDLLDMFGPDRLPRLVSYGDGSAIEDPVMALIGEAYEACAVRFEWRKGDVVMLDNMLAAHARDPYEEPRLIVVAMGEMTARGDVWQPA | Cell lysis | [84,85,86,87,88] |
SyrP protein | ||||
Iturin A | Bacillus subtilis | KIYGVYMDRPLSAGEEVRMMAAVSAEKREKCRRFYHKEDAHRTLIGDMLIRTAAAKAYGLDPAGISFGVQEYGKPYIPALPDMHFNISHSGRWIVCAVDSKPIGIDIEKMKPGTIDIAKRFFSPTEYSDLQAKHPDQQTDYFYHLWSMKESFIKQAGKGLSLPLDSFSVRLKDDGHVSIEL | Cell lysis | [86,88,89] |
Nikkomycin | Streptomyces spp. | Inhibition of chitin biosynthesis | [90,91,92] | |
Pepstatin A | Streptomyces spp. | Inhibition of aspartic proteases | [92] | |
Fungal Peptides | ||||
Aculeacin A | Aspergillus aculeatus | Inhibition of 1,3-β-d-glucan synthase | [92,93] | |
Plant Peptides | ||||
Defensins | ||||
Rs-AFP1 | Raphanus sativus | QKLCERPSGTWSGVCGNNNACKNQCINLEKARHGSCNYVFPAHKCICYFPC | Membrane permeabilization | [62,88,94,95,96] |
Rs-AFP2 | QKLCQRPSGTWSGVCGNNNACKNQCIRLEKAWGSCNYVFPAHKCICYFPC | |||
Thionins | ||||
CaThi | Capsicum annuum | KEICCKVPTTPFLCTNDPQCKTLCSKVNYEDGHCFDILSKCVCMNRCVQDAKTLAAELIEEEFLKQ | Membrane permeabilization | [88,97,98] |
Thaumatin-like (TL) proteins | ||||
Osmotin | Nicotiana tabacum | ATIEVRNNCPYTVWAASTPIGGGRRLDRGQTWVINAPRGTKMARVWGRTNCNFNAAGRGTCQTGDCGGVLQCTGWGKPPNTLAEYALDQFSGLDFWDISLVDGFNIPMTFAPTNPSGGKCHAIHCTANINGECPRELRVPGGCNNPCTTFGGQQYCCTQGPCGPTFFSKFFKQRCPDAYSYPQDDPTSTFTCPGGSTNYRVIFCPNGQAHPNFPLEMPGSDEVAK | Cell wall perturbations; spore lysis | [86,88,99,100] |
Zeamatin | Zea mays | AAVFTVVNQCPFTVWAASVPVGGGRQLNRGESWRITAPAGTTAARIWARTGCKFDASGRGSCRTGDCGGVLQCTGYGRAPNTLAEYALKQFNNLDFFDISLIDGFNVPMSFLPDGGSGCSRGPRCAVDVNARCPAELRQDGVCNNACPVFKKDEYCCVGSAANDCHPTNYSRYFKGQCPDAYSYPKDDATSTFTCPAGTNYKVVFCP | Cell lysis | |
Insect Peptides | ||||
Cecropins | ||||
Stomoxyn | Stomoxys calcitrans | RGFRKHFNKLVKKVKHTISETAHVAKDTAVIAGSGAAVVAAT | Cell lysis | [54,88,101] |
Melittin | Apis mellifera | GIGAVLKVLTTGLPALISWIKRKRQQ-CONH2 | Proapoptotic activity | [102,103] |
Defensins | ||||
Drosomycin | Drosophila melanogaster | DCLSGRYKGPCAVWDNETCRRVCKEEGRSSGHCSPSLKCWCEGC | Cell lysis | [86,88,104] |
Tenecin 3 | Tenebrio molitor | DHHDGHLGGHQTGHQGGQQGGHLGGQQGGHLGGHQGGQPGGHLGGHQGGIGGTGGQQHGQHGPGTGAGHQGGYKTHGH | Unknown | [71,88,105] |
Holotricin 3 | Holotrichia diomphalia | YGPGDGHGGGHGGGHGGGHGNGQGGGHGHGPGGGFGGGHGGGHGGGGRGGGGSGGGGSPGHGAGGGYPGGHGGGHHGGYQTHGY | Growth inhibition | |
Termicin | Pseudacanthotermes spiniger | ACNFQSCWATCQAQHSIYFRRAFCDRSQCKCVFVRG | ||
Amphibian Peptides | ||||
Magainin 2 | Xenopus laevis | GIGKFLHSAKKFGKAFVGEIMNS | Disrubtion of plasma membrane | [106,107,108] |
Buforin I | Bufo bufo garagriozans | AGRGKQGGKVRAKAKTRSSRAGLQFPVGRVHRLLRKGNY | Cell lysis | [55,106] |
Buforin II | TRSSRAGLQFPVGRVHRLLRK | |||
Temporin A | Rana temporaria | FLPLIGRVLSGIL | Cell lysis | [56,88,109] |
Dermaseptin-1 | Phyllomedusa hypochondrialis | GLWSTIKNVGKEAAIAAGKAALGAL | Membrane permeabilization | [86,88,110,111] |
Avian Peptides | ||||
Avian β-defensins | ||||
Gallinacins | Gallus gallus | GRKSDCFRKSGFCAFLKCPSLTLISGKCSRFYLCCKRIWG | Cell lysis | [86,88,112,113,114,115] |
β-defensin-4 | IVLLFVAVHGAVGFSRSPRYHMQCGYRGNFCTPGKCPHGNAYPGLCRPKYSCCRW | |||
THP-1 | Meleagris gallopavo | GKREKCLRRNGFCAFLKCPTLSVISGTCSRFQVCC | ||
Spheniscin-1 | Aptenodytes patagonicus | SFGLCRLRRGFCAHGRCRFPSIPIGRCSRFVQCCRRVW | ||
Cathelicidins | ||||
Cathelicidin-2 | Gallus gallus | LVQRGRFGRFLRKIRRFRPKVTITIQGSARFG | Cell lysis | [88,116] |
Mammalian Peptides | ||||
α-defensins | ||||
HNP-1 | Homo sapiens | ACYCRIPACIAGERRYGTCIYQGRLWAFCC | Cell lysis | [86,88,117,118] |
HNP-2 | CYCRIPACIAGERRYGTCIYQGRLWAFCC | |||
NP-1 | Rabbit bocaparvovirus | MSSRHSPYPRKTSGDTTGSKTSWASSGSRENKGNHKNPSFSTASRPFLTRQQKKEILKPRALRKDPPKVFCATHRADSPDAPAVCGFFWHSNRIAGKGTDWIFTRGKQLFQERAKNNVIDWDMARDLLFSFKRECDQWYRNMLYHFRLGEPCDKCNYWDGAYRKYCARVNADYEKEINATSASQELTDEEAAAALDAAMADASH | ||
β-defensins | ||||
HBD-1 | Homo sapiens | DHYNCVSSGGQCLYSACPIFTKIQGTCYRGKAKCCK | Cell lysis | [88,118,119,120] |
HBD-2 | TCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP | |||
HBD-3 | GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGKCSTRGRKCCRRKK | |||
HBD-4 | ELDRICGYGTARCRKKCRSQEYRIGRCPNTYACCLRK | |||
Tracheal antimicrobial peptide (TAP) | Bos taurus | MRLHHLLLALLFLVLSAWSGFTQGVGNPVSCVRNKGICVPIRCPGSMKQIGTCVGRAVKCCRKK | ||
Lingual antimicrobial peptide (LAP) | VRNSQSCRRNKGICVPIRCPGSMRQIGTCLGAQVKCCRRK | |||
θ-defensins | ||||
RTD-1 | Macaca mulatta | GFCRCLCRRGVCRCICTR | Cell lysis | [88,121,122] |
Cathelicidins | ||||
LL-37 | Homo sapiens | LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES | Destabilization of plasma membrane | [88,123] |
Indolicidin | Bos taurus | ILPWKWPWWPWRR | Destabilization of plasma membrane | [88,124,125,126] |
Tritrpticin | Sus scrofa | VRRFPWWWPFLRR | Destabilization of plasma membrane | [88,127] |
Protegrin-1 | RGGRLCYCRRRFCVCVGR | Destabilization of plasma membrane | [88,124,128] | |
Histatins | ||||
Histatin-5 | Homo sapiens | DSHAKRHHGYKRKFHEKHHSHRGY | Osmotic stress | [88,129,130,131] |
Lactoferrin-derived peptides | ||||
Lactoferricin H | Homo sapiens | GRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQA | Disruption of plasma membrane | [88,132,133,134,135] |
Lactoferricin B | Bos taurus | FKCRRWQWRMKKLGAPSITCVRRAF |
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Bondaryk, M.; Staniszewska, M.; Zielińska, P.; Urbańczyk-Lipkowska, Z. Natural Antimicrobial Peptides as Inspiration for Design of a New Generation Antifungal Compounds. J. Fungi 2017, 3, 46. https://doi.org/10.3390/jof3030046
Bondaryk M, Staniszewska M, Zielińska P, Urbańczyk-Lipkowska Z. Natural Antimicrobial Peptides as Inspiration for Design of a New Generation Antifungal Compounds. Journal of Fungi. 2017; 3(3):46. https://doi.org/10.3390/jof3030046
Chicago/Turabian StyleBondaryk, Małgorzata, Monika Staniszewska, Paulina Zielińska, and Zofia Urbańczyk-Lipkowska. 2017. "Natural Antimicrobial Peptides as Inspiration for Design of a New Generation Antifungal Compounds" Journal of Fungi 3, no. 3: 46. https://doi.org/10.3390/jof3030046