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Animal‐Derived Bioactive Peptides as Next‐Generation Therapeutics

A Special Issue of International Journal of Molecular Sciences (ISSN 1422-0067) belonging to the section "Molecular Toxicology".

Deadline for manuscript submissions: closed (30 June 2026) | Viewed by 1290

Editors


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Guest Editor
1. Laboratory of Toxinology, Physiological Sciences Department, Biological Sciences Institute, University of Brasilia, Brasilia 70910‐900, DF, Brazil
2. Laboratory of Protein Chemistry and Biochemistry, Cellular Biology Department, Biological Sciences Institute, University of Brasilia, Brasilia 70910‐900, DF, Brazil
Interests: amphibians; peptide chemistry; antimicrobial peptides; peptide synthesis; peptide analogues; anti‐inflammatory peptides; wound‐healing; antiparasitic therapies
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Guest Editor
Laboratory of Protein Chemistry and Biochemistry, Department of Cell Biology, Institute of Biological Sciences, University of Brasilia, Brasilia 70910‐900, DF, 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,

Animal venoms, poisons, and skin secretions represent some of the richest and most evolutionarily refined biological reservoirs of bioactive compounds. Over millions of years,

venomous and poisonous animals—including snakes, scorpions, spiders, amphibians, cone snails, insects, and fish—have developed complex molecular arsenals for predation and defense. Among these components, peptides stand out as highly potent, selective, and structurally diverse molecules, offering an unparalleled source of novel therapeutic leads. Their natural stability, specificity for distinct molecular targets, and broad spectrum of biological activities position these peptides as exceptional candidates for innovative drug development.

Animal‐derived bioactive peptides represent one of the most promising frontiers in the development of new antimicrobial, anti‐inflammatory, wound‐healing, and antiparasitic therapies. In the face of the continuous rise in microbial resistance, the limitations of conventional antibiotics, and the urgent need for safer and more selective therapeutic alternatives, these peptides emerge as highly versatile candidates, combining rapid microbicidal properties, low likelihood of resistance development, and significant immunomodulatory capacity. A wide variety of organisms—including amphibians, insects, fish, mollusks, and mammals—produce peptides that are integral components of natural defense mechanisms, offering efficient molecular templates for the creation of innovative therapeutics.

Beyond their antimicrobial activity, numerous toxin‐derived peptides exhibit relevant anti‐inflammatory effects, modulating key pathways of both the innate and adaptive immune systems. These compounds have also demonstrated considerable potential as wound‐healing agents, promoting cell proliferation, angiogenesis, and tissue remodeling. In parallel, antiparasitic peptides originating from venoms and toxic secretions have emerged as attractive alternatives for neglected diseases, often acting through mechanisms distinct from those of conventional pharmacological therapies.

This Special Issue aims to integrate multidisciplinary knowledge, gather recent discoveries, and stimulate innovative approaches positioning venom‐, poison‐, and secretion-derived peptides as next‐generation therapeutic agents. The proposal seeks to consolidate current advances and guide new perspectives for the translational and clinical application of these bioactive molecules.

We invite researchers from diverse fields (including molecular biology, biochemistry, toxinology, pharmacology, immunology, peptide chemistry, and biotechnology) to submit original research articles, reviews, communications, and perspectives that align with the themes of this Special Issue. Submissions addressing emerging therapeutic strategies, novel biological models, or technological innovations related to toxin‐derived peptides are particularly encouraged.

Potential topics for this Special Issue include, but are not limited to, the following:

  • Anti‐inflammatory properties and modulation of innate immune pathways by venom/secretion peptides.
  • Molecular mechanisms of action of antimicrobial and immunomodulatory peptides derived from venoms, poisons, and skin secretions.
  • Wound‐healing peptides from amphibian skin secretions, venom glands, and other toxin‐producing systems.
  • Peptides with antiparasitic activity and new approaches for neglected diseases based on toxin‐derived scaffolds.
  • Anti‐inflammatory properties and modulation of innate immune pathways by venom/secretion peptides.
  • Rational mutations and structure–function relationships in antimicrobial, immunomodulatory, and wound‐healing peptides of toxic origin.
  • Stabilization strategies (D‐amino acids, cyclization, conjugation, lipidation) applied to toxin‐derived peptides.
  • Innovative formulations (nanoparticles, hydrogels, delivery systems) that enhance the therapeutic potential of venom‐based peptides.
  • Advanced mechanistic studies using mass spectrometry, NMR, microscopy, and omics analyses in toxin‐derived peptide research.
  • Crosstalk between toxin‐derived peptides and immune cells (neutrophils, macrophages, keratinocytes).
  • Therapeutic applications, new preclinical and in vivo models, and translational perspectives for venom‐ or animal secretion‐derived peptides.

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

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Keywords

  • venom-derived peptides
  • animal toxins
  • antimicrobial peptides
  • immunomodulation
  • wound healing
  • antiparasitic agents
  • peptide‐based therapeutics
  • skin secretions

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Published Papers (1 paper)

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Research

25 pages, 3562 KB  
Article
A Novel Ocellatin-P1 Isoform from Leptodactylus labyrinthicus Frog Skin Secretion: Purification, Biological Properties and Three-Dimensional Structure
by César Augusto Prías-Márquez, Eliane Santana Fernandes Alves, Carlos José Correia de Santana, Osmindo Rodrigues Pires Júnior, Eduardo Maffud Cilli, Fabiano José Queiroz Costa, Alice da Cunha Morales Álvares, Sonia Maria de Freitas, Isabel de Fátima Correia Batista, Rafael Marques Porto, Isabelle S. Luz, Ricardo B. Azevedo, João Paulo Stawiarski Miranda, Henrique de Oliveira Noronha, Marco Antônio Damasceno Faustino, Felipe da Silva Mendonca de Melo, Alexandra Maria dos Santos Carvalho, Izabela Marques Dourado Bastos, Wagner Fontes, Aline L. Oliveira, Luciano M. Lião and Mariana S. Castroadd Show full author list remove Hide full author list
Int. J. Mol. Sci. 2026, 27(8), 3658; https://doi.org/10.3390/ijms27083658 - 20 Apr 2026
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Abstract
A novel ocellatin-P1 isoform was isolated and purified from the skin secretion of the pepper frog Leptodactylus labyrinthicus. The crude skin secretion was fractionated by reversed-phase high-performance liquid chromatography (RP-HPLC) using a C8 column and the peptide was subsequently purified on [...] Read more.
A novel ocellatin-P1 isoform was isolated and purified from the skin secretion of the pepper frog Leptodactylus labyrinthicus. The crude skin secretion was fractionated by reversed-phase high-performance liquid chromatography (RP-HPLC) using a C8 column and the peptide was subsequently purified on a reversed-phase C18 column. Ocellatin-LB3 (as this isoform was named) was chemically sequenced by Edman degradation. This peptide is a linear C-terminally amidated molecule composed of 25 amino acid residues: 1GLLDTLKGAAKNVVGGLASKVMEKL25-NH2. Synthetic ocellatin-LB3 was active against Escherichia coli, Klebsiella pneumoniae and Pseudomonas aeruginosa and inactive against Staphylococcus aureus, Staphylococcus epidermidis and Enterococcus faecalis. In addition, the peptide reduced the Trypanosoma cruzi infection in L6 cells. At 64 µM it did not reduce erythrocytes or polymorphonuclear leukocytes, but did reduce mononuclear leukocyte counts, as detected by flow cytometry. No hemolytic activity was observed in red blood cells even at 128 µM. The peptide exhibited limited antiproliferative activity against MCF-7 and HeLa tumor cells at 128 µM. Pre-incubation with the peptide appeared to enhance N-formylmethionine-leucyl-phenylalanine (fMLP)-induced migration, indicating a potential additive or synergistic effect on human neutrophils. The three-dimensional structure of ocellatin-LB3 was investigated by circular dichroism (CD) and nuclear magnetic resonance (NMR). In the presence of sodium dodecyl sulfate (SDS), the peptide adopts an α-helical structure spanning residues Leu3–Lys24, which remains largely preserved even at 95 °C. NMR Hydrogen/Deuterium (H/D) exchange experiments suggest that ocellatin-LB3 adopts a preferential orientation when interacting with SDS micelles. Based on the similarity among ocellatins, and on the physicochemical and structural properties of this peptide, a possible membrane-mediated mode of action is proposed, although this remains to be experimentally validated. Full article
(This article belongs to the Special Issue Animal‐Derived Bioactive Peptides as Next‐Generation Therapeutics)
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