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Review

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Laboratory of Biochemistry and Biotechnology, Institute for Marine Sciences, Federal University of Ceara, Fortaleza 60165-081, Brazil
Received: 28 December 2020 / Revised: 31 January 2021 / Accepted: 9 February 2021 / Published: 15 February 2021
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). View Full-Text
Keywords: cell-penetrating peptide; venom peptide; arachnid venom peptide; insect venom peptide; snake venom peptide; cellular uptake; peptide chemical modification; peptide engineering; peptide design; peptide carrier cell-penetrating peptide; venom peptide; arachnid venom peptide; insect venom peptide; snake venom peptide; cellular uptake; peptide chemical modification; peptide engineering; peptide design; peptide carrier
MDPI and ACS Style

Rádis-Baptista, G. Cell-Penetrating Peptides Derived from Animal Venoms and Toxins. Toxins 2021, 13, 147. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13020147

AMA Style

Rádis-Baptista G. Cell-Penetrating Peptides Derived from Animal Venoms and Toxins. Toxins. 2021; 13(2):147. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13020147

Chicago/Turabian Style

Rádis-Baptista, Gandhi. 2021. "Cell-Penetrating Peptides Derived from Animal Venoms and Toxins" Toxins 13, no. 2: 147. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13020147

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