Special Issue "Cell-Penetrating Peptides Derived from Animal Venoms and Toxins: Origins, Structures, Multifunctionalities and Advances"
Deadline for manuscript submissions: closed (31 December 2020).
Interests: transcriptome of arthropods, cnidarians and other venomous animals; peptide engineering; anti-proliferative peptides; membranolytic peptides; pharmaceutical biotechnology
Special Issues and Collections in MDPI journals
Special Issue in Toxins: Toxinologic and Pharmacological Investigation of Venomous Arthropods
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
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 papers will be 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 2400 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.
- animal venom
- cell-penetrating peptides
- membrane-translocating peptide
- peptide toxin
- therapeutic peptide
- theranostic agents
- venom-derived peptides