Vipericidins, Snake Venom Cathelicidin-Related Peptides, in the Milieu of Reptilian Antimicrobial Polypeptides

Rádis‐Baptista, Gandhi

doi:10.1007/978-94-007-6410-1_2

Cited by 2 publications

(2 citation statements)

References 163 publications

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“…Vipericidins, in general and crotalicidin, in particular, are surprisingly similar to previously characterized Asian elapid CRAMPs, despite South American pit vipers and Asian elapids (cobras and kraits) being geographically and phylogenetically distant venomous snake groups, which evolutionarily diverged millions of years ago. Multiple biological activities have been reported for crotalicidin, vipericidin-related sequences and elapid CRAMPs, with emphasis on antipathogenic and antitumoral properties, as reviewed elsewhere [ 135 , 155 , 156 , 157 ]. The antimicrobial activity ranges from multidrug-resistant clinical isolates to life-threatening viruses, as reported for cathelicidin-OH30 derived from the venom of the king cobra Ophiophagus hannah, as well as venom cathelicidin-BF30 and short derivatives from the banded krait Bungarus fasciatus venom [ 158 , 159 ].…”

Section: Cell-penetrating Peptides From Animal Venoms and Toxinsmentioning

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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Section: Cell-penetrating Peptides From Animal Venoms and Toxinsmentioning

confidence: 99%

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Rádis‐Baptista

2021

Toxins

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“…Ctn (KRFKKFFKKVKKSVKKRLKKIFKKPMVIGVTIPF), Ctn [1][2][3][4][5][6][7][8][9][10][11][12][13][14] (KRFKKFFKKVKKSV), and Ctn [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34] (KKRLKKIFKKPMVIGVTIPF) were synthesized by solid phase methods, purified by HPLC to >95% homogeneity, and characterized by ESI-mass spectrometry, as previously described Figure 6. Depicted mechanism of action of Ctn [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29]…”

Section: Peptidesmentioning

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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Vipericidins, Snake Venom Cathelicidin-Related Peptides, in the Milieu of Reptilian Antimicrobial Polypeptides

Cited by 2 publications

References 163 publications

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

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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