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Toxins
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Cell-Penetrating Peptides Derived from Animal Venoms and Toxins: Origins, Structures,...
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Cell-Penetrating Peptides Derived from Animal Venoms and Toxins: Origins, Structures, Multifunctionalities and Advances

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 9978

Special Issue Editors

Prof. Dr. Gandhi Rádis-Baptista

E-Mail Website
Guest Editor
Laboratory of Biochemistry and Biotechnology, Institute for Marine Sciences, Federal University of Ceara, Fortaleza 60165-081, CE, Brazil
Interests: transcriptome of arthropods, cnidarians and other venomous animals; peptide engineering; anti-proliferative peptides; membranolytic peptides; regulatory peptides; molecular biology; pharmaceutical biotechnology
Special Issues, Collections and Topics in MDPI journals
Prof. John Howl

E-Mail Website
Guest Editor
Research Institute in Healthcare Science, University of Wolverhampton
Interests: biology and chemistry of peptides, cell-penetrating peptides, and peptide antibiotics

Special Issue Information

Dear Colleagues,

Cell-penetrating peptides (CPPs) comprise a class of short polypeptides that possess the exquisite capabilities of binding selectively to the membrane of certain cell types, translocate across lipid bilayers, penetrate and home to cell cytoplasm, organelles and specific subcellular compartments. With such intrinsic properties, along the process of membrane translocation and cellular uptake, CPPs can versatilely carry covalently attached to their N- and C-termini, or physically complexed, macromolecules (nucleic acids and proteins), nanoparticles (nanocrystals and magnetic beads), hydrophilic organic compounds, metals and radionuclides. They are natural in their origin, made up of domains, parts or patches of larger proteins, as well as can comprise sequences that are de novo designed and synthesized. One of the best examples of CPPs are the short Tat fragments (e.g., Tat(47-57) or Tat(48-60)) of the transactivator of transcription (Tat protein) from the HIV-1 and penetratin (Antp(43-58)), the segment of the antennapedia (Antp) homeodomain from the fruit fly Drosophila. A limited number of animal toxins, isolated mainly from the venoms of arthropod and reptile, were demonstrated to have cell-penetrating activity, despite their unrelated structures. Concomitantly, these venom-derived CPPs display a variable spectrum of antitumoral and anti-infective effects. For instance, crotamine from the venom of South American rattlesnake, chlorotoxin and maurocalcine from scorpion venom, mastoparan from the venom of wasps and melittin from the honeybee venom have been investigated, in their unmodified (naïve) or engineered designed derivates, for application in imaging diagnostics, intracellular tracking/trafficking, drug delivery and targeted therapies of tumors. Based on the richness of venom–peptide activities, this Special Issue is focused on the origin, structures and multifunctionalities of CPPs that are derived from animal venom and toxins. Moreover, it is intended to bring together the recent advances on the application of venom-derived CPPs for clinical diagnostic and therapeutic intervention of chronic and infectious diseases.

Prof. Gandhi Rádis-Baptista
Prof. John Howl
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • animal venom
  • cell-penetrating peptides
  • membrane-translocating peptide
  • peptide toxin
  • therapeutic peptide
  • theranostic agents
  • venom-derived peptides

Published Papers (2 papers)

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Review

25 pages, 487 KiB  
Review
Cell-Penetrating Peptides Derived from Animal Venoms and Toxins
by Gandhi Rádis-Baptista
Toxins 2021, 13(2), 147; https://doi.org/10.3390/toxins13020147 - 15 Feb 2021
Cited by 30 | Viewed by 5325
Abstract
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 [...] Read more.
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). Full article
(This article belongs to the Special Issue Cell-Penetrating Peptides Derived from Animal Venoms and Toxins: Origins, Structures, Multifunctionalities and Advances)
18 pages, 855 KiB  
Review
Drug Delivery Strategies for Enhancing the Therapeutic Efficacy of Toxin-Derived Anti-Diabetic Peptides
by Reeju Amatya, Taehoon Park, Seungmi Hwang, JaeWook Yang, Yoonjin Lee, Heesun Cheong, Cheol Moon, Hyun Duck Kwak, Kyoung Ah Min and Meong Cheol Shin
Toxins 2020, 12(5), 313; https://doi.org/10.3390/toxins12050313 - 10 May 2020
Cited by 11 | Viewed by 3920
Abstract
Toxin peptides derived from the skin secretions of amphibians possess unique hypoglycemic activities. Many of these peptides share cationic and amphipathic structural similarities and appear to possess cell-penetrating abilities. The mechanism of their insulinotropic action is yet not elucidated, but they have shown [...] Read more.
Toxin peptides derived from the skin secretions of amphibians possess unique hypoglycemic activities. Many of these peptides share cationic and amphipathic structural similarities and appear to possess cell-penetrating abilities. The mechanism of their insulinotropic action is yet not elucidated, but they have shown great potential in regulating the blood glucose levels in animal models. Therefore, they have emerged as potential drug candidates as therapeutics for type 2 diabetes. Despite their anti-diabetic activity, there remain pharmaceutical challenges to be addressed for their clinical applications. Here, we present an overview of recent studies related to the toxin-derived anti-diabetic peptides derived from the skin secretions of amphibians. In the latter part, we introduce the bottleneck challenges for their delivery in vivo and general drug delivery strategies that may be applicable to extend their blood circulation time. We focus our research on the strategies that have been successfully applied to improve the plasma half-life of exendin-4, a clinically available toxin-derived anti-diabetic peptide drug. Full article
(This article belongs to the Special Issue Cell-Penetrating Peptides Derived from Animal Venoms and Toxins: Origins, Structures, Multifunctionalities and Advances)
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