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Toxins
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Animal Toxins as a Remarkable Source for Drug Discovery and...
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Animal Toxins as a Remarkable Source for Drug Discovery and Development

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

Deadline for manuscript submissions: closed (31 August 2023) | Viewed by 5671

Special Issue Editors

Prof. Dr. Mariana S. Castro

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Guest Editor
Toxinology Laboratory, Department of Physiological Sciences, Institute of Biology, University of Brasilia, Brasilia 70.910-900, Brazil
Interests: amphibians; peptide chemistry; antimicrobial peptides; peptide synthesis; peptide analogues; neurotoxic peptides; scorpions
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Wagner Fontes

E-Mail Website
Guest Editor
Laboratory of Protein Chemistry and Biochemistry, Department of Cell Biology, Institute of Biological Sciences, University of Brasilia, Brasilia 70910-900, Brazil
Interests: biologically active peptides; peptide engineering; analogs; toxins-based drug discovery; proteomics; neutrophils
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Poisons and venoms are complex mixtures of salts, small organic molecules, peptides and proteins that are produced by animals for self-defense, predation or intraspecific competition. Poisonous and venomous animals are widely distributed in Nature, including invertebrates such as cnidarians, mollusks, annelids, hymenopterans, and spiders; and vertebrates such as snakes, platypus, amphibians, lizards, and fishes. Several venom/poison toxins have been studied as pharmacological tools and bioinsecticides, and for therapeutic purposes due to their biological and pharmacological properties, including antimicrobial, anticancer, antiparasitic, analgesic, wound-healing, antihypertensive, and neuroprotective effects. This Special Issue will accept original research articles and reviews that highlight the potential of toxins found in animal venoms and poisons as prototypes or templates for the development of new therapeutic agents for the treatment of several diseases and disorders (e.g., type 2 diabetes mellitus, cancer, microbial infections, chronic pain, thrombotic diseases, neurodegenerative diseases).

Prof. Dr. Mariana S. Castro
Prof. Dr. Wagner Fontes
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

  • venoms
  • poisons
  • animal toxins
  • biologically active peptides
  • drug discovery and development
  • toxin-based drug discovery
  • therapeutic applications

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Published Papers (2 papers)

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Research

17 pages, 4768 KiB  
Article
Revitalizing Skin Repair: Unveiling the Healing Power of Livisin, a Natural Peptide Calcium Mimetic
by Xuehui Zhan, Danni Wang, Hanfei Wang, Hui Chen, Xinyi Wu, Tao Li, Junmei Qi, Tianbao Chen, Di Wu and Yitian Gao
Toxins 2024, 16(1), 21; https://doi.org/10.3390/toxins16010021 - 31 Dec 2023
Cited by 1 | Viewed by 2196
Abstract
When the skin is damaged, accelerating the repair of skin trauma and promoting the recovery of tissue function are crucial considerations in clinical treatment. Previously, we isolated and identified an active peptide (livisin) from the skin secretion of the frog Odorrana livida. [...] Read more.
When the skin is damaged, accelerating the repair of skin trauma and promoting the recovery of tissue function are crucial considerations in clinical treatment. Previously, we isolated and identified an active peptide (livisin) from the skin secretion of the frog Odorrana livida. Livisin exhibited strong protease inhibitory activity, water solubility, and stability, yet its wound-healing properties have not yet been studied. In this study, we assessed the impact of livisin on wound healing and investigated the underlying mechanism contributing to its effect. Our findings revealed livisin effectively stimulated the migration of keratinocytes, with the underlying mechanisms involved the activation of CaSR as a peptide calcium mimetic. This activation resulted in the stimulation of the CaSR/E-cadherin/EGFR/ERK signaling pathways. Moreover, the therapeutic effects of livisin were partially reduced by blocking the CaSR/E-cadherin/EGFR/ERK signaling pathway. The interaction between livisin and CaSR was further investigated by molecular docking. Additionally, studies using a mouse full-thickness wound model demonstrated livisin could accelerate skin wound healing by promoting re-epithelialization and collagen deposition. In conclusion, our study provides experimental evidence supporting the use of livisin in skin wound healing, highlighting its potential as an effective therapeutic option. Full article
(This article belongs to the Special Issue Animal Toxins as a Remarkable Source for Drug Discovery and Development)
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16 pages, 2331 KiB  
Article
Evaluation of the Synthetic Multifunctional Peptide Hp-MAP3 Derivative of Temporin-PTa
by Patrícia Souza e Silva, Alexya Sandim Guindo, Pedro Henrique Cardoso Oliveira, Luiz Filipe Ramalho Nunes de Moraes, Ana Paula de Araújo Boleti, Marcos Antonio Ferreira, Caio Fernando Ramalho de Oliveira, Maria Ligia Rodrigues Macedo, Luana Rossato, Simone Simionatto and Ludovico Migliolo
Toxins 2023, 15(1), 42; https://doi.org/10.3390/toxins15010042 - 5 Jan 2023
Viewed by 2624
Abstract
In recent years, antimicrobial peptides isolated from amphibian toxins have gained attention as new multifunctional drugs interacting with different molecular targets. We aimed to rationally design a new peptide from temporin-PTa. Hp-MAP3 (NH2-LLKKVLALLKKVL-COOH), net charge (+4), hydrophobicity (0.69), the content of [...] Read more.
In recent years, antimicrobial peptides isolated from amphibian toxins have gained attention as new multifunctional drugs interacting with different molecular targets. We aimed to rationally design a new peptide from temporin-PTa. Hp-MAP3 (NH2-LLKKVLALLKKVL-COOH), net charge (+4), hydrophobicity (0.69), the content of hydrophobic residues (69%), and hydrophobic moment (0.73). For the construction of the analog peptide, the physicochemical characteristics were reorganized into hydrophilic and hydrophobic residues with the addition of lysines and leucines. The minimum inhibitory concentration was 2.7 to 43 μM against the growth of Gram-negative and positive bacteria, and the potential for biofilm eradication was 173.2 μM. Within 20 min, the peptide Hp-MAP3 (10.8 μM) prompted 100% of the damage to E. coli cells. At 43.3 μM, eliminated 100% of S. aureus within 5 min. The effects against yeast species of the Candida genus ranged from 5.4 to 86.6 μM. Hp-MAP3 presents cytotoxic activity against tumor HeLa at a concentration of 21.6 μM with an IC50 of 10.4 µM. Furthermore, the peptide showed hemolytic activity against murine erythrocytes. Structural studies carried out by circular dichroism showed that Hp-MAP3, while in the presence of 50% trifluoroethanol or SDS, an α-helix secondary structure. Finally, Amphipathic Hp-MAP3 building an important model for the design of new multifunctional molecules. Full article
(This article belongs to the Special Issue Animal Toxins as a Remarkable Source for Drug Discovery and Development)
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