A Comprehensive Review of Patented Antimicrobial Peptides from Amphibian Anurans

García, Fabiola Almeida; Fuentes, Talia Frómeta; Alonso, Isel Pascual; Bosch, Roberto Alonso; Brunetti, Andrés E.; Lopes, Norberto Peporine

doi:10.1021/acs.jnatprod.3c01040

Cited by 5 publications

(3 citation statements)

References 119 publications

(285 reference statements)

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Section: Discussionmentioning

confidence: 99%

“…AMPs from anurans have been studied for the last four decades, and interest in them has increased with the global health emergency of antimicrobial resistance. It has been shown that anuran AMPs are targets of patents that propose their development as new drugs, including through bioengineering involving amino acid modifications [20]. In this work, we performed the fractionation of skin secretion from L. vastus (LSV) from the Brazilian northeast and ended up isolating a new peptide belonging to the group of ocellatins.…”

Section: Discussionmentioning

confidence: 99%

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First Report of Ocellatin-VT from the Skin Secretion of Leptodactylus vastus Lutz (Amphibia: Leptodactylidae)

Silva,

Barbosa,

Santana

et al. 2024

Chemistry

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The global emergency of antimicrobial resistance has drawn several efforts to evaluate new drug candidates, such as natural defensive biomolecules. Ocellatins are a group of antimicrobial peptides found in anurans of the Leptodactylidae family. This work investigated the presence of antimicrobial peptides in the skin secretion of Leptodactylus vastus from the Brazilian northeast. The secretion was fractionated by RP-HPLC, and the fractions were screened for antibacterial activity. A peptide isolated from the most active fraction was characterized for primary structure and evaluated for antibacterial activity, cytotoxicity to murine melanoma cells (B16-F10), and hemolytic activity. The RP-HPLC profile displayed 26 fractions, with fraction 25 being the most active. One of the two peptides present in this fraction had the primary structure determined, belonging to the group of ocellatins. Since it was not identical to other ocellatins previously reported, it was named ocellatin-VT. This peptide especially inhibited Gram-negative bacteria growth, with the highest activity against Acinetobacter baumannii and Escherichia coli (growth inhibition was higher than 95% at 8 and 16 µM, respectively). Ocellatin-VT was weakly cytotoxic to B16-F10 cells and showed low hemolytic activity. In conclusion, a new ocellatin was isolated from L. vastus skin secretion that was active against non-resistant and multidrug-resistant bacteria.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

First Report of Ocellatin-VT from the Skin Secretion of Leptodactylus vastus Lutz (Amphibia: Leptodactylidae)

Silva,

Barbosa,

Santana

et al. 2024

Chemistry

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“…Since the pioneering studies by the Erspamer group, it has been well-established that anuran skin secretion harbors a diverse array of compounds, exhibiting a wide spectrum of biological activity. − Among these compounds are host defense peptides (HDPs), known for their capability to inhibit bacterial growth and demonstrating remarkable diversity in their bioactivity spectrum against a wide range of microorganisms. − These molecules hold significant potential for drug development. , …”

mentioning

confidence: 99%

First Bioprospecting Study of Skin Host-Defense Peptides in Odontophrynus americanus

Cancelarich,

Arrulo,

Gugliotti

et al. 2024

J. Nat. Prod.

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The adaptation of amphibians to diverse environments is closely related to the characteristics of their skin. The complex glandular system of frog skin plays a pivotal role in enabling these animals to thrive in both aquatic and terrestrial habitats and consists of crucial functions such as respiration and water balance as well as serving as a defensive barrier due to the secretion of bioactive compounds. We herein report the first investigation on the skin secretion of Odontophrynus americanus, as a potential source of bioactive peptides and also as an indicator of its evolutionary adaptations to changing environments. Americanin-1 was isolated and identified as a neutral peptide exhibiting moderate antibacterial activity against E. coli. Its amphipathic sequence including 19 amino acids and showing a propensity for α-helix structure is discussed. Comparisons of the histomorphology of the skin of O. americanus with other previously documented species within the same genus revealed distinctive features in the Patagonian specimen, differing from conspecifics from other Argentine provinces. The presence of the Eberth−Katschenko layer, a prevalence of iridophores, and the existence of glycoconjugates in its serous glands suggest that the integument is adapted to retain skin moisture. This adaptation is consistent with the prevailing aridity of its native habitat.

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Unlocking the Potential of Antimicrobial Maximin Peptides From Bombina maxima Against Staphylococcus aureus: Deciphering Their Mode of Action Through a Mimetic Bacterial Membrane Environment

Vinutha,

Rajasekaran

2024

Peptide Science

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Antimicrobial peptides (AMPs) offer a promising strategy to address bacterial resistance by targeting bacterial membranes, bypassing the limitations of receptor site‐based approaches. This study focuses on combating the notorious multidrug resistance of Staphylococcus aureus using AMPs, particularly maximin peptides derived from Bombina maxima. Previous research suggested that maximin peptides could disrupt bacterial membranes among anuran AMPs. This prompted us to screen these maximin peptides to identify those with strong membrane‐targeting abilities against S. aureus. Initially, stability and activity assessments on all 89 peptides involved analyzing hydrogen bond dilution, peptide permeation, and hemolytic activity predictions, leading to the rationalization of four promising candidates: Max_5, Max_13, Max_21, and Max_45. When subjected to membrane simulations, the monomeric state of these peptides displayed partial helix‐coil transitions with significant structural interactions that disrupted the membrane, particularly for Max_5 and Max_13. Additionally, the multimeric states of these two peptides were examined through membrane simulations to elucidate their mechanisms of action. Analyses focusing on membrane thickness, lipid distortions, and curvature revealed that both Max_5 and Max_13 exerted strong membrane‐rupturing effects. These peptides seemed to operate by forming pores, facilitating lipid diffusion, creating cavities, and affecting membrane thickness, which allowed water penetration due to increased membrane fluidity, indicating the barrel‐stave pore model. Despite structural differences between Max_5 and Max_13, both peptides demonstrated similar outcomes, emphasizing their potential for future therapeutic applications. This study highlights the efficacy of computational methods in accelerating the identification of potent antimicrobial peptides, providing a pathway for developing novel antimicrobial therapies.

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A Comprehensive Review of Patented Antimicrobial Peptides from Amphibian Anurans

Cited by 5 publications

References 119 publications

First Report of Ocellatin-VT from the Skin Secretion of Leptodactylus vastus Lutz (Amphibia: Leptodactylidae)

First Report of Ocellatin-VT from the Skin Secretion of Leptodactylus vastus Lutz (Amphibia: Leptodactylidae)

First Bioprospecting Study of Skin Host-Defense Peptides in Odontophrynus americanus

Unlocking the Potential of Antimicrobial Maximin Peptides From Bombina maxima Against Staphylococcus aureus: Deciphering Their Mode of Action Through a Mimetic Bacterial Membrane Environment

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