Biotechnological
Communication
Biosci. Biotech. Res. Comm. 11(3): 376-386 (2018)
Antifungal peptides: Biosynthesis, production and
applications
Narjis Fathima Mirza
1
, Snehasri Motamarry
1
, Preetha Bhadra
2
and Bishwambhar Mishra
2
*
1
Department of Biotechnology, Sreenidhi Institute of Science and Technology, Ghatkesar, Hyderabad–501301,
India
2
Department of Biotechnology, Centurion University of Technology and Management, Bhubaneswar–752050
India
ABSTRACT
Fungal infections in animal, plants and fungal contamination of food for humans and livestock result in substantial
worldwide economic losses. In the last few years, fungal infection has increased strikingly by a rise in the number
of deaths of acquired immunode ciency syndrome (AIDS) cancer patients, transplant patients owing to fungal infec-
tions. The growth rate of fungi is very slow as compared to bacteria and very dif cult to identify. Approximately 100
peptides have been investigated to date for their antifungal properties, which can be of great importance to overcome
the human diseases. Insects secrete such compounds, which can be peptides, as a part of their immune defense reac-
tions. Antifungal peptides are excellent models for drug discovery exhibiting unique characteristics such as high
speci city, broad spectrum, low level of resistance reaching and unique mode of action. The aim of this review is to
provide information on research on these important peptides.
KEY WORDS: ANTIFUNGAL; PEPTIDES; MODE OF ACTION; FUNGAL INFECTION; FUNGI CIDAL
376
ARTICLE INFORMATION:
*Corresponding Author: mishra.bishwambhar@gmail.com
Received 11
th
July, 2018
Accepted after revision 27
th
Sep, 2018
BBRC Print ISSN: 0974-6455
Online ISSN: 2321-4007 CODEN: USA BBRCBA
Thomson Reuters ISI ESC / Clarivate Analytics USA and
Crossref Indexed Journal
NAAS Journal Score 2018: 4.31 SJIF 2017: 4.196
© A Society of Science and Nature Publication, Bhopal India
2018. All rights reserved.
Online Contents Available at: http//www.bbrc.in/
DOI: 10.21786/bbrc/11.3/5
INTRODUCTION
Many research advances have been made in medicine at
present. Be it in the treatment of HIV-AIDS, cancer, or
organ transplantation, the success rates have increased
drastically over past 50 years. Even though success rates
have been increased, many patients are left with compro-
mised immune systems (Wisplinghoff etal., 2004). The
Patients, receiving chemotherapy, organ transplantation,
use of prosthetic Devices and vascular catheters, dialysis
etc., are easily susceptible to manybacterial, viral and
fungal infections (Spellberg etal., 2008). Even though
fungal species are serious pathogens, they get lesser
attention when compared to bacterial and viral infec-
Narjis Fathima Mirza etal.
tions as, the frequency of occurrence of fungal infec-
tions has been comparatively less to bacterial and viral
infections (Georgopapadakou etal., 1996; Wisplinghoff
et al., 2004; Porto et al., 2012). Human fungal infec-
tions, caused by Aspergillus fumigatus, Cryptococcusne-
oformans, Candida albicans, are increasing in a number
o mmune-compromised patients (Blanco et al., 2008).
Fungal pathogens such as Candida species and Aspergil-
lus species are more common and account up to 19%
of cases (Schelenz etal., 2009). C. albicans is known as
major fungal pathogen and is 4
th
most common cause of
nosocomial infections (Banerjee etal., 1991; Beck-Sague
etal., 1993; Wisplinghoff etal., 2004; Xiao etal., 2013;
Chen etal., 2016; Ageitos etal., 2017; Bondaryk etal.,
2017).
Only a limited number of antifungal drugs are avail-
able such as echinocandins, polyenes etc., (Gupte etal.,
2002). Amphotericin B, which was discovered in 1956,
is still used for treatment many fungal infections. Just
like bacterial resistance, fungal pathogens have also
developed resistance in past 20 years. (Gold etal., 2002;
Georgopapadakou etal., 1996). The fact that fungal and
bacterial infections are different and bacterial infec-
tions are treated more easily is because, fungal cells are
eukaryotic and bacterial cells are prokaryotic. The main
concern in treating fungal infections is that any chemi-
cal substance that is successful in damaging the eukary-
otic cell wall of fungi may also cause possible damage
to human cells, unlike antibiotics, which won’t have
any effect on humans. Any chemical substance that is
toxic to fungus may also be toxic to humans (Moham-
mad et al., 2015). Therefore, there is need to discover
new biochemical targets in fungi. Antifungal peptides
are treatment alternatives, derived from natural sources
and are effective against fungal infections, thus, safe for
immune compromised patients (Gold etal., 2002; Ravi
etal., 2011; Thakur etal., 2012; Jia etal., 2016; Wang
etal., 2016; Veltri etal., 2017).
Antifungal peptides from natural sources are much
cheaper than commercial antifungal drugs and are
also better alternative to combat resistance. Antifungal
peptides are cationic biomolecules with weight around
1.3 kDa to 30 kDa (Mohammad etal., 2015). Antifun-
gal peptides are classi ed into two types based on their
mode of action. First group are, lytic peptides, (Rees
etal., 1997; Shai etal., 1995). These peptides are amphi-
pathic in nature (contain a positive and a neutral charge)
and disrupt the membrane structure by  xing onto its
surface (Leuschner etal., 2004; Shai etal., 1995). The
second group of peptides act by inhibiting the synthesis
of cell wall or essential cell wall components such as
glucan, chitin (Fernández etal., 2004; Lata etal., 2010;
Joseph et al., 2012; Liu et al., 2016; Bondaryk et al.,
2017).
SOURCES OF ANTIFUNGAL PEPTIDES
Bacterial Peptides Iturins
Iturin was one of  rst antifungal peptides, ever iso-
lated. It is produced by different strains of Bacillus sub-
tilis (Georgopapadakou et al., 1996). They are cyclic
lipopeptides and act by disrupting the cell membrane
of fungi, hence leaking its vital ions (XinZhao et al.,
2013; Lemaitre etal., 1997). Iturin A, of iturin family,
was observed to inhibit A.  avus and F. moniliforme
growth and had Minimal inhibitory concentration (MIC)
of 22.0 μg/ml against Saccharomyces cerevisiae. It was
found to be effective against dermatomycoses. (De Lucca
etal., 1999). But iturin A was also observed to be hemo-
lytic. Bacillomycin F, another family member of iturin,
is known to inhibit strains such as Byssochlamys fulva,
A.niger, C.albicans, and F.oxysporumand had MIC of
40.0μg/ml for A.niger (De Lucca etal., 1999). Bacillo-
mycin D produced by Bacillus amyloliquefaciens was
found to be effective against a plant pathogenic fungi
Fusarium graminearum and Candida species. MIC of
(12.5-25) μg/ml was observed against various Candida
species (Tabbene etal., 2015; Qin Gu etal., 2017).
Syringomycins: Syringomycins are produced by Pseu-
domonas syringae are small cyclic lipodepsipeptides with
ergosterol as a binding site in yeast. The most prevalent of
Syringomycinsis syringomycin-E (SE) which was found to
be lethal to many strains such as A.  avus, A. fumigatus,
A.niger, F. moniliforme and F. oxysporum showing LD95
of 1.9 μg/ml. it showed MIC of (0.8–12.5) μg/ml against
C. neoformans (De Lucca et al., 1999). Syringotoxin B,
syringostantin A which were lipodepsinonapeptides were
found to be effective against Candida, Cryptococcus, and
Aspergillus species. Syringostantin A had MIC of 5.0μg/
ml against A. fumigatus. Syringotoxin B had MIC of
3.2μg/ml against C. albicans (Sorensen etal., 1996; Zhao
etal., 2013; Chereddy etal., 2014; Deslouches etal., 2015;
Gao etal., 2016; Kubicek-Sutherland etal., 2017).
Pseudomycins: Pseudomycins, another family, structur-
ally related to syringomycins also have antifungal activ-
ity against wide ranges of species. Existing as pseudomy-
cins (A, B, and C), these have shown antifungal activity
against Ceratocystis ulmi, C. Albicans, Rynchosporium
secalis,Rhizoctonia solani,Sclerotiniasclerotiorum Ver-
ticillium albo-atrum, Verticillium dahliae, Thielavio-
pis basicola, F. oxysporum, F. culmorum. The MIC of
pseudomycin A, against C. neoformans was 1.56 μg/ml
whereas 3.12 μg/ml was observed against C. albicans
(De Lucca etal., 1999).
Plant Peptides: Large number of antifungal peptides are
identi ed from plant sources, but only few were tested
and found to be effective.
BIOSCIENCE BIOTECHNOLOGY RESEARCH COMMUNICATIONS ANTIFUNGAL PEPTIDES: BIOSYNTHESIS, PRODUCTION AND APPLICATIONS 377
Narjis Fathima Mirza etal.
Table 1. Antifungal peptides from bacterial sources
Peptide name Family/group Structure source
Fungal species
effected
Typical
target
organism
Mode of
action
In vitro
MIC (μg/
ml)
Reference
Bacillomycin F Iturins lipopeptide B. subtilis.
Byssochlamys fulva,
A. niger, C.albicans,
and F.oxysporum
A. niger lysis 40
(De Lucca etal.,
1999; Bionda etal.,
2016)
iturin A Iturins lipopeptide
Bacillus
amyloliquefaciens
A.  avus, F.
moniliforme, S.
cerevisiae
S. cerevisiae lysis 22.0
(Georgopapadakou
etal., 1996; De
Lucca etal., 1999;
Brandenburg etal.,
2015)
bacillomycin D Iturins lipopeptide
Bacillus
amyloliquefaciens
F. graminearum and
Candida species.
Candida
species
lysis 12.50-25.0
(Tabbene etal.,
2015; Qin Gu etal.,
2017,)
syringomycin-E (SE)
Syringomycins
lipodepsipeptide
Pseudomonas
syringae
A.  avus, A.
fumigatus, A.niger,
F. moniliforme and
F. oxysporum
C.
neoformans
lysis 0.8–12.5
(De Lucca etal.,
1999; Falciani etal.,
2014)
syringostantin A
Syringomycins
lipodepsinonapeptides
Pseudomonas
syringae
Candida,
Cryptococcus, and
Aspergillus species
A. fumigatus lysis 5.0
(Sorensen etal.,
1996; Falciani etal.,
2014)
Syringotoxin B
Syringomycins
Lipodepsinonapeptide
Pseudomonas
syringae
Candida,
Cryptococcus, and
Aspergillus species.
C. albicans lysis 3.2
(Sorensen etal.,
1996; Lyu etal.,
2016)
pseudomycin A Pseudomycins lipodepsinonapeptides
Pseudomonas
syringae
C. albicans, F.
oxysporum , F.
culmorum, C.
neoformans
C. albicans lysis 3.12
(De Lucca etal.,
1999; Brunetti etal.,
2016)
378 ANTIFUNGAL PEPTIDES: BIOSYNTHESIS, PRODUCTION AND APPLICATIONS BIOSCIENCE BIOTECHNOLOGY RESEARCH COMMUNICATIONS
Narjis Fathima Mirza etal.
Table 2. Antifungal peptides from plant sources
Peptide name Family/group
No. of
amino acids
source
Target
organism
In vitro MIC
(μg/ml)
Reference
Ib-AMP3 Plant defensins 20
Impatiens
balsamina
F. moniliforme 50.0
(De Lucca etal., 1999;
Asano etal., 2013)
Frangufoline Cyclopeptides *534
Rhamnus
frangula
A. niger 5.0
(Gournelis etal., 1997;
De Lucca 2000; Tan
etal., 2006; Choe
etal., 2015)
Rugosanine A
Cyclopeptides
*585 Ziziphus rugosa A. niger 5.0
(Gournelis etal.,
1997; De Lucca 2000;
Tan etal., 2006; Cole
etal., 2016)
Nummularine
Cyclopeptides
*587
Ziziphus
nummularia
A. niger 5.0
(Gournelis etal., 1997;
De Lucca 2000; Tan
etal., 2006; Dobson
etal., 2014)
ACE-AMP1
Lipid transfer
proteins
93 Allium cepa L F. oxysporum 10.0
(De Lucca 2000; Dutta
etal., 2015)
Table 3. Antifungal peptides from fungal sources
Peptide name Structure source
Typical target
organism
Mode of action
In vitro MIC
(μg/ml)
Reference
Caspofungin lipopeptide G.lozoyensis Candida spp glucan synthesis 8 - 64
(Bartizaletal.,
1997;Groll etal.,
1999; Kuhn
etal., 2002;
Deresinski etal.,
2003; Porto
etal., 2012)
Anidulafungin
(LY303366)
Lipopeptide A. nidulans Candida spp glucan synthesis 0.5 - 4.0
(Lucca etal.,
1999; Denning
etal., 1997;
Ghannoum etal.,
2005; De Lei
etal., 2013)
Cilofungin (LY121019) Lipopeptide A. nidulans C. albicans Glucan synthesis 0.62
(De Lucca 2000;
Joseph etal.,
2012)
Echinocandin B Lipopeptide A. nidulans C. albicans Glucan synthesis 0.625
(De Lucca 2000;
Veltri etal.,
2017)
Aculeacin Lipopeptide
A.
aculeatus C. albicans
Glucan synthesis 0.2
(De Lucca etal.,
1999; Chen
etal., 2016)
Trichopolyn
Amino-
lipopeptide
Trichoderma
polysporum C. albicans Unknown
0.8 (De Lucca 2000;
Liu etal., 2016)
Leucinostatin
Amino-
lipopeptide
Penicillium
lilacinum
C. neoformans
Unknown
0.5
(De Lucca 2000;
Zhao etal.,
2013 )
Plant defensins
Plant defensins are eight disul de-linked cysteines with
a single helix and triple-stranded b-sheet (Bruix etal.,
1995). Ib-AMP
3
, isolated from Impatiens balsamina, was
observed to be lethal against germinated conidia of A.
avus by 42%, where as it was non-lethal against non-
germinated conidia.It had MIC of 50.0μg/ml against
F. moniliforme (De Lucca et al., 1999; Asano et al.,
2013).
BIOSCIENCE BIOTECHNOLOGY RESEARCH COMMUNICATIONS ANTIFUNGAL PEPTIDES: BIOSYNTHESIS, PRODUCTION AND APPLICATIONS 379
Narjis Fathima Mirza etal.
Table 5. Antifungal peptides from amphibian sources
Peptide name
No. of amino
acids
source
Typical Target
organism
Mode of
action
In vitro MIC
(μg/ml)
Reference
Magainin 2
23 Xenopus laevis C. albicans
Lysis 80.0
(Zasloff etal.,
2002; Bondaryk
etal., 2017)
Dermaseptin b 27
Phyllomedusa
sauvagii
C.
neoformans
Lysis
60.0
(Landon
etal., 1997;
Brandenburg
etal., 2015)
Dermaseptin s 34 P. sauvagii C. neoformans Lysis
5.0
(Landon etal.,
1997; Brunetti
etal., 2016)
Skin-PYY (SPYY)
36 P. bicolor A. fumigatus
Membrane
permiation
80.0
(Vouldoukis etal.,
1996; Brunetti
etal., 2016)
Brevinin-2R 24 Rana ridibunda C. albicans 3.0
(Conlon
etal., 2003;
Anunthawan
etal., 2015 )
Cyclopeptides: Cyclopeptides from different species of
Rhamnaceae family were observed to have antifungal
activities. Frangufoline, from barks of Rhamnus fran-
gula were observed to have anti-bacterial and anti-
fungal properties. It showed MIC of 5.0 μg/ml for A.
niger. Nummularine (B, K, R, and S), from stem barks
of Ziziphus nummularia, Rugosanine (A and B) from
stem barks of Ziziphus rugosa and abyssenine-C from
stem barks of Ziziphus abyssinica, were all observed to
have antifungal properties against A. niger with MIC of
5 μg/ml. However, they were observed to be well effec-
tive against A. niger but not against C. albicans and
their mechanism of action was also unknown (Gournelis
etal., 1997; De Lucca 2000; Tan etal., 2006).
Lipid transfer proteins and other peptides: ACE-
AMP1 is a lipid transfer protein, produced by seeds of
Allium cepa which was observed to be effective against
F. oxysporum with MIC of 10.0 μg/ml (Cammue etal.,
1995; De Lucca 2000). Apart from the above antifun-
gal peptides, some other peptides include, Chitinases
and glucanases, which hydrolyze chitin, glucan, and
Table 4. Antifungal peptides from insect sources
Peptide
name
Family/group
No. of
amino acids
source
Typical Target
organism
Mode of
action
In vitro
MIC (μg/
ml)
Reference
Cecropin A
Cecropins
37 Hyalopora cecropia F. oxysporum, lysis 12.4
(De Lucca
etal.,1998;
Joseph etal.,
2012)
Cecropin B
Cecropins
35 Hyalopora cecropia
A. fumigatus
lysis 9.5
(Nappi etal.,
2001; Xiao
etal., 2013)
Drosomycin
Cysteine-rich
peptides
44
Drosophila
melanogaster and
Podisus maculiveris
F.oxysporum lysis 5.9
(De Lucca,
2000; Veltri
etal., 2017)
Thanatin
Cysteine-rich
peptides
21
Podisus
maculiveris F. oxysporum Unknown
5.0
(Bulet etal.,
2005; Wang
etal., 2015)
Heliomicins
Insect Defensins 44
Heliothis
virescens
C. neoformans
Unknown
12.0
Nappi etal.,
2001; De Lucca
2000; Zhao
etal., 2013;
Ageitos etal.,
2017)
380 ANTIFUNGAL PEPTIDES: BIOSYNTHESIS, PRODUCTION AND APPLICATIONS BIOSCIENCE BIOTECHNOLOGY RESEARCH COMMUNICATIONS
Narjis Fathima Mirza etal.
the essential cell wall components of fungi. Prematins,
members of PR-5 protein family, act by permeabilizing
fungal membranes. Similarly, Thionins inhibit by per-
meabilizing fungal membranes and were found to be
effective against F. graminearum and F. sporotrichioides
(Velazhahan etal., 2001; Asano etal., 2013).
Fungal Peptides: Antifungal peptides from fungi
are more active than those compared to bacteria and
plants. Echinocandins are lipopeptides which inhibit
1,3--glucan synthase (Gregory etal., 2007). Glucan is
the major component of cell wall of fungi and inhibi-
tion of glucan may result in osmotic instability and in
cell lysis. (Lee etal., 1995; Gregory etal., 2007; Osorio
etal., 2015; Liu etal., 2016). The MIC90 value of echi-
nocandins was found to be ≤2 μg/mL against Candida
spp (Zaas etal., 2005). A-192411.29 had anti- fungicidal
activity against C. albicans, C. tropicalis and C. glabrata
(Vazquez et al., 2005; Kaconis etal., 2011; Chu et al.,
2013). But, the echinocandins do not show any antifun-
gal activity against Cryptococcus spp, Trichosporon spp,
Fusarium spp, zygomycetes (Zaas etal., 2005; Kazemza-
deh-Narbat etal., 2010). They also, do not affect human
cells, as human cells do not contain 1,3--D-glucan.
However, echinocandins are labeled category C and
are toxic to embryos (Gregory etal., 2007; Lakshmaiah
Narayana etal., 2014).
Micafungin from Coleophoma empedra, caspofungin
from Glarea lozoyensis and anidulafungin from A.
nidulans of echinocandin family have been approved
so far (Murdoch etal., 2004; Montgomery etal., 2013).
Of these, anidulafungin displays least MIC values fol-
lowed by micafungin and caspofungin being most. This
was observed against Candida spp. (Zaas et al., 2005;
Mojsoska etal., 2015). Caspofungin, also known as (MK-
0991) is a second generation pneumocandin from Glarea
lozoyensis (Abruzzo et al., 1997; Groll et al., 1999;
López-Garcia etal. 2005; Popovic etal., 2012 ). It was
fungicidal against C.albicans and C. parapsilosis (Bar-
tizal et al., 1997; Kuhn et al., 2002; Deresinski et al.,
2003; Ordonez etal., 2014 ). It was observed be effec-
tive against hyphal tips A. fumigatus although not com-
pletely lethal (Krishnan etal., 2005). It was also lethal
against several molds such as Alternaria sp., Curvularia
sp., Acremonium sp., Bipolaris sp., and Trichodermasp
(Kahn et al., 2006). Micafungin also known as FK463
had antifungal activity against disseminated candidi-
asis and aspergillosis (Petraitisetal., 2000; Lakshmaiah
Narayana etal., 2015).
The optimal concentration of FR463 at single infu-
sion was observed to be 2.5-25 mg (Azuma etal., 1998;
Pettengell etal., 1999; Kasetty etal., 2015; Kang etal.,
2017). Anidulafungin (V-echinocandin), previously
known as LY303366 is a semisynthetic echinocandin
currently used as antifungal drug (Krause etal., 2004;
Harder et al., 2013; Kang et al., 2017).It is a lipopep-
tide produced by A. nidulans, (Lei etal., 2013) and acts
by inhibiting glucan synthase (Denning et al., 1997;
Anunthawan etal., 2015). It was observed to be effec-
tive against Candidemia and other Candida infections
and esophageal candidiasis. MIC of (0.5 to 4.0) μg/ml
was observed in Candida spp. However, Anidulafungin
displays low MICs against strains of C. parapsilosis and
is not effective inactive against C. neoformans and Blas-
tomyces dermatitidis (De Lucca etal., 1999; Ghannoum
etal., 2005; Ben Lagha etal., 2017).
Echinocandin B from A. nidulans and A. rugulosus
was effective against C. albicans with MIC of 0.625 μg/
ml. Cilofungin (LY121019), isolated from Aspergillus
spp. had MIC of 0.62 μg/ml. Amino-lipopeptides such as
Trichopolyns from Trichoderma polysporum have MIC
of (0.78 - 6.25) μg/ml for C. albicans. Other families of
potent antifungal peptides include the leucinostatins
and helioferins families also consist of antifungal pop-
erties, but, where toxic, hemolytic to mammalian cells in
vitro (De Lucca 2000; Lei etal., 2013; Osorio etal., 2015;
Chen etal., 2016; Ageitos etal., 2017).
Insect Peptides: Cecropins
Cecropins (A and B) are linear lytic peptides, made up
of an 11- amino acid sequence, produced in hemolymph
giant silk moth, Hyalopora cecropia. Cecropin B was
observed lethal against F. oxysporum (approximately
95%), A. fumigatus 9.5 μg/ml (De Lucca et al., 1998;
Nappi etal., 2001). cecropin A was observed to be more
fungicidal at neutral pH and was more affective against
Fusarium moniliforme and Fusarium oxysporum with
total killing of 12.4 μg/ml (De Lucca etal.,1998).
Drosomycin: Drosomycin is a Cysteine-rich peptide
containing 44 amino acid with a twisted three-stranded
sheet structure steadied by disul de bonds. It is isolated
from Drosophila melanogaster and Podisus maculiveris
and was found to be effective against F.oxysporum with
MIC value of 5.9 μg/ml (De Lucca, 2000 ).
Glycin-rich peptides
Antifungal peptides, such as holotricin-3, and tenecin-3
are glycine-rich peptides isolated from insects (Nappi
etal., 2001). Tenecin-3 was studied to be effective against
C. albicans (Ganz, 2003). Holotricin-3, was isolated from
larval hemolymph of Holotrichia diomphalia, and was
observed to inhibit C. albicans growth (Lee etal., 1995).
Thanatin:Thanatin is another non-hemolytic Cysteine-
rich peptide containing 21 amino acid residues and
is smaller compared to drosomycin. It was affective
against many strains such as Trichoderma viride, Alter-
naria brassicola, Neurospora crassa, Botrytis cinerea,
and Fusarium culmorum, A. fumigatusT. mentagro-
BIOSCIENCE BIOTECHNOLOGY RESEARCH COMMUNICATIONS ANTIFUNGAL PEPTIDES: BIOSYNTHESIS, PRODUCTION AND APPLICATIONS 381
Narjis Fathima Mirza etal.
phytes and F. oxysporum (Fehlbaum etal., 1996; Bulet
etal., 2005). MIC of 5.0 μg/ml was observed against F.
oxysporum. However Thanatin was not effective against
yeast (Mandard etal., 1998).
Heliomicin: Heliomicin from Heliothis virescens
(tobacco budworm), was observed to have antifungal
activity against C. neoformans, with MIC of 12.0 μg/ml
(De Lucca 2000; Nappi etal., 2001).
Amphibian Peptides: Magainins: Magainins was the
rst among the antifungal peptides from amphib-
ian sources. They are amphiphilic, non-hemolytic and
are produced by Xenopus laevis (African clawed frog).
Magainin 2 inhibited C. albicans growth and had MIC of
80.0 μg/ml (De Lucca etal., 1999; Zasloff etal., 2002).
Dermaseptins: Dermaseptins are linear, lytic,peptides
produced by Phyllomedusa sauvagii (South American
arboreal frog). Dermaseptin was lethal towards for A.
avus, A. fumigatus, and F. oxysporum, with LD50
values observed as 3 μM, 0.5 μM, and 0.8 μM, respec-
tively (Landon etal., 1997). Dermaseptin b was effective
against yeasts and some  lamentous fungi such as C.
neoformansand had MIC value of 60.0μg/ml. Dermasep-
tin s had MIC of 5.0μg/mlfor C. neoformans. (De Lucca
etal., 1999).
Skin-PYY (SPYY): Skin-PYY (SPYY), is an antifungal
compound produced by Phyllomedusa bicolor (South
American tree frog). It was observed to inhibit C. neo-
formans, C. albicans, and A. fumigatus and had MIC val-
ues of 20 μg/ml, 15 μg/ml, and 80 μg/ml, respectively
(Vouldoukis etal., 1996).
Brevinin: Brevinin-2R isolated from skin of Rana
ridibunda (red frog). It is non-hemolytic, 24 amino acid
peptide with -helical conformation. It was observed to
have MIC of 3.0 μg/ml against C. albicans (Conlon etal.,
2003).
FUTURE PROSPECTS
Emerging fungal resistance to conventional therapies
necessitates the development of novel antifungal strate-
gies. In this context, Anti-fungal peptides draw the atten-
tion as alternative potential antifungal agents (Brunetti
etal., 2016). These peptides are relatively safe, tolerated
and highly effective. As per the information available in
the literatures, only few antifungal peptides are used in
antifungal therapy (Brandenburg etal., 2015). There are
various problems addressed which is limiting the uses
of these peptides, such as low bioavailability, hemolytic
activity, instability, high cost of production, possible
aggregation, loss of activity in high salt concentrations,
poor ability to cross physiological barriers (Chen etal.,
2016; Ageitos etal., 2017).
Due to these effects, the therapeutic use of antifungal
peptides is signi cantly decreased now a day. However,
the utilization of these peptides could be enhanced by
chemical optimization and new delivery strategies. With
the advancement of new research strategies, the wide
variety of natural antimicrobial peptides should be char-
acterized both structurally and functionally for making
them extremely promising source of ideas in design the
novel antifungal peptides. In particular, application of
dendrimers as scaffolds for assembling well de ned
macromolecular polyvalent molecules or synthesis de
novo of per se active linear and branched peptide mim-
ics makes them extremely promising for use as new gen-
eration antifungal peptides.As found in several studies,
the modes of antifungal action must be well understood
(Deslouches et al., 2015; Gao et al., 2016; Kubicek-
Sutherland etal., 2017). Hopefully, all these efforts will
result in the development of a novel class of antifungal
agents to their full potential.
CONCLUSION
Antifungal peptides are excellent models for drug dis-
covery exhibiting unique characteristics such as low
level of resistance reaching the absent, high speci city,
broad spectrum, and unique mode of action. Despite the
distinctiveness, only few examples of antifungal pep-
tides have successfully reached the market.
ACKNOWLEDGEMENTS
All the authors want to acknowledge Sreenidhi Institute
of Science and Technology, Hyderabad and Centurion
University, Bhubaneswar for providing digital library to
explore the information to execute this work.
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