The antiproliferative peptide Ctn[15‐34] is active against multidrug‐resistant yeasts<i>Candida albicans</i>and<i>Cryptococcus neoformans</i>

Aguiar, Francisca Lidiane Linhares de; Cavalcante, Carolina Sidrim de Paula; Fontenelle, Raquel Oliveira dos Santos; Falcão, Cláudio Borges; Andreu, David; Rádis‐Baptista, Gandhi

doi:10.1111/jam.14493

Cited by 12 publications

(23 citation statements)

References 50 publications

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“…Similar, although not yet understood, synergistic or additive effects of fluconazole with various AMPs against Candida spp. strains (especially FLC-resistant fungi) were reported [30][31][32][33][34][35]. It was claimed that combination of different compounds as described above could be one of the most promising approach as to develop alternative therapy against multidrug resistant or biofilmforming yeast-like fungi.…”

Section: Discussionmentioning

confidence: 99%

“…On the basis of this development, it has been postulated that both compounds (Omiganan and retro-Omiganan) could effectively be used in the treatment of Candida infections associated with biofilm. Moreover, there are few studies that indicate synergistic anti-Candida effect of combination of azoles (e.g., fluconazole) with various AMPs [30][31][32][33][34][35]. This effect could probably be associated with different mechanisms of action of both groups of compounds.…”

Section: Introductionmentioning

confidence: 99%

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Anticandidal Activity of Omiganan and Its Retro Analog Alone and in Combination with Fluconazole

Czechowicz

Jaśkiewicz

Neubauer

et al. 2021

Probiotics & Antimicro. Prot.

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Vulvovaginal candidiasis (VVC) is a vaginal infection that manifests itself as several symptoms which can lead to various life-threatening complications. The majority of VVC is caused by Candida albicans strains, and it is estimated that approximately 75% of women worldwide would suffer from this condition at least once during their lifetime. Surprisingly, the detailed pathomechanism of yeast-like fungi invasions in vagina is not yet fully understood. However, the ability to form biofilm on vaginal mucosa is considered as one of the critical factors associated with failure of the therapy and recurrences of the disease. Antimicrobial peptides (AMPs) are a promising class of compounds that are receiving a growing interest owing to their antibacterial, antifungal, and antibiofilm properties. Omiganan is a synthetic analog of Indolicidin that is characterized by wide spectrum of antimicrobial and antibiofilm activities. Recent reports suggest improved activity of analogs with a reversed sequence (retro-analog concept). Therefore, Omiganan and its retro analog were tested against planktonic forms and biofilm of 18 Candida strains isolated from VVC. Moreover, the synergy between the AMPs and fluconazole was studied as well. The AMPs appeared to be effective against C. albicans biofilm, and the reversion of the sequence generally led to an improved antimicrobial activity. Furthermore, confocal and scanning electron microscopic visualizations revealed the effectiveness of AMPs-fluconazole combinations also against fluconazole-resistant strains. Graphical Abstract

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Anticandidal Activity of Omiganan and Its Retro Analog Alone and in Combination with Fluconazole

Czechowicz

Jaśkiewicz

Neubauer

et al. 2021

Probiotics & Antimicro. Prot.

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“…The anti-inflammatory properties of venom cathelicidins have also been observed in in vitro and in vivo models of inflammation for cathelicidin-BF30 [160] and for CRAMPs from the venom of the blue-banded sea snake Hydrophis cyanocyntus, demonstrating the potent antimicrobial activity, associated with immunomodulatory effects of snake venom cathelicidins [161,162]. Short peptide fragments of snake venom cathelicidins have been prepared, displaying different levels of activity and efficacy against a range of microbes, including viruses [163], multidrug-resistant bacteria, pathogenic yeasts and biofilms [164][165][166][167].…”

Section: Crotalicidin and Elapid Crampsmentioning

confidence: 99%

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Rádis‐Baptista

2021

Toxins

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Cell-penetrating peptides (CPPs) comprise a class of short polypeptides that possess the ability to selectively interact with the cytoplasmic membrane of certain cell types, translocate across plasma membranes and accumulate in the cell cytoplasm, organelles (e.g., the nucleus and mitochondria) and other subcellular compartments. CPPs are either of natural origin or de novo designed and synthesized from segments and patches of larger proteins or designed by algorithms. With such intrinsic properties, along with membrane permeation, translocation and cellular uptake properties, CPPs can intracellularly convey diverse substances and nanomaterials, such as hydrophilic organic compounds and drugs, macromolecules (nucleic acids and proteins), nanoparticles (nanocrystals and polyplexes), metals and radionuclides, which can be covalently attached via CPP N- and C-terminals or through preparation of CPP complexes. A cumulative number of studies on animal toxins, primarily isolated from the venom of arthropods and snakes, have revealed the cell-penetrating activities of venom peptides and toxins, which can be harnessed for application in biomedicine and pharmaceutical biotechnology. In this review, I aimed to collate examples of peptides from animal venoms and toxic secretions that possess the ability to penetrate diverse types of cells. These venom CPPs have been chemically or structurally modified to enhance cell selectivity, bioavailability and a range of target applications. Herein, examples are listed and discussed, including cysteine-stabilized and linear, α-helical peptides, with cationic and amphipathic character, from the venom of insects (e.g., melittin, anoplin, mastoparans), arachnids (latarcin, lycosin, chlorotoxin, maurocalcine/imperatoxin homologs and wasabi receptor toxin), fish (pardaxins), amphibian (bombesin) and snakes (crotamine and cathelicidins).

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“…After the first report of the presence of cecropins in the hemolymph of Hyalophora cecropia moths [1], in 1981, reports followed of mammalian α-defensins in human neutrophils [2] and magainins in the skin secretions of the amphibian Xenopus laevis four years later [3]. The expression of antimicrobial peptides (AMPs) in organisms of all kingdoms has been recognized as an essential feature of the innate immunity system, and hundreds of AMP sequences belonging to different structural and dynamic light scattering, zeta potential assays, confocal microscopy, and atomic force microscopy, the membrane selectivity is demonstrated and new insights on the mechanism of action of Ctn [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34] against C. albicans are revealed.…”

Section: Introductionmentioning

confidence: 99%

Antibiofilm Activity on Candida albicans and Mechanism of Action on Biomembrane Models of the Antimicrobial Peptide Ctn[15–34]

Aguiar

Santos

Cavalcante

et al. 2020

IJMS

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Ctn[15–34], the C-terminal fragment of crotalicidin, an antimicrobial peptide from the South American rattlesnake Crotalus durissus terrificus venom, displays remarkable anti-infective and anti-proliferative activities. Herein, its activity on Candida albicans biofilms and its interaction with the cytoplasmic membrane of the fungal cell and with a biomembrane model in vitro was investigated. A standard C. albicans strain and a fluconazole-resistant clinical isolate were exposed to the peptide at its minimum inhibitory concentration (MIC) (10 µM) and up to 100 × MIC to inhibit biofilm formation and its eradication. A viability test using XTT and fluorescent dyes, confocal laser scanning microscopy, and atomic force microscopy (AFM) were used to observe the antibiofilm effect. To evaluate the importance of membrane composition on Ctn[15–34] activity, C. albicans protoplasts were also tested. Fluorescence assays using di-8-ANEPPS, dynamic light scattering, and zeta potential measurements using liposomes, protoplasts, and C. albicans cells indicated a direct mechanism of action that was dependent on membrane interaction and disruption. Overall, Ctn[15–34] showed to be an effective antifungal peptide, displaying antibiofilm activity and, importantly, interacting with and disrupting fungal plasma membrane.

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The antiproliferative peptide Ctn[15‐34] is active against multidrug‐resistant yeastsCandida albicansandCryptococcus neoformans

Cited by 12 publications

References 50 publications

Anticandidal Activity of Omiganan and Its Retro Analog Alone and in Combination with Fluconazole

Anticandidal Activity of Omiganan and Its Retro Analog Alone and in Combination with Fluconazole

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Antibiofilm Activity on Candida albicans and Mechanism of Action on Biomembrane Models of the Antimicrobial Peptide Ctn[15–34]

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