Journal articles: 'Amphibian peptides'

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Wang, Guangshun. "Bioinformatic Analysis of 1000 Amphibian Antimicrobial Peptides Uncovers Multiple Length-Dependent Correlations for Peptide Design and Prediction." Antibiotics 9, no. 8 (August 7, 2020): 491. http://dx.doi.org/10.3390/antibiotics9080491.

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Amphibians are widely distributed on different continents, except for the polar regions. They are important sources for the isolation, purification and characterization of natural compounds, including peptides with various functions. Innate immune antimicrobial peptides (AMPs) play a critical role in warding off invading pathogens, such as bacteria, fungi, parasites, and viruses. They may also have other biological functions such as endotoxin neutralization, chemotaxis, anti-inflammation, and wound healing. This article documents a bioinformatic analysis of over 1000 amphibian antimicrobial peptides registered in the Antimicrobial Peptide Database (APD) in the past 18 years. These anuran peptides were discovered in Africa, Asia, Australia, Europe, and America from 1985 to 2019. Genomic and peptidomic studies accelerated the discovery pace and underscored the necessity in establishing criteria for peptide entry into the APD. A total of 99.9% of the anuran antimicrobial peptides are less than 50 amino acids with an average length of 24 and a net charge of +2.5. Interestingly, the various amphibian peptide families (e.g., temporins, brevinins, esculentins) can be connected through multiple length-dependent relationships. With an increase in length, peptide net charge increases, while the hydrophobic content decreases. In addition, glycine, leucine, lysine, and proline all show linear correlations with peptide length. These correlations improve our understanding of amphibian peptides and may be useful for prediction and design of new linear peptides with potential applications in treating infectious diseases, cancer and diabetes.

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CHEN, Tianbao, Susan FARRAGHER, Anthony J. BJOURSON, David F. ORR, Pingfan RAO, and Chris SHAW. "Granular gland transcriptomes in stimulated amphibian skin secretions." Biochemical Journal 371, no. 1 (April 1, 2003): 125–30. http://dx.doi.org/10.1042/bj20021343.

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Amphibian defensive skin secretions are complex, species-specific cocktails of biologically active molecules, including many uncharacterized peptides. The study of such secretions for novel peptide discovery is time-limited, as amphibians are in rapid global decline. While secretion proteome analysis is non-lethal, transcriptome analysis has until now required killing of specimens prior to skin dissection for cDNA library construction. Here we present the discovery that polyadenylated mRNAs encoding dermal granular gland peptides are present in defensive skin secretions, stabilized by endogenous nucleic acid-binding amphipathic peptides. Thus parallel secretory proteome and transcriptome analyses can be performed without killing the specimen in this model amphibian system—a finding that has important implications in conservation of biodiversity within this threatened vertebrate taxon and whose mechanistics may have broader implications in biomolecular science.

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Cao, Xiaoqing, Jing Tang, Zhe Fu, Zhuo Feng, Siyuan Wang, Meifeng Yang, Chunyun Wu, Ying Wang, and Xinwang Yang. "Identification and Characterization of a Novel Gene-encoded Antioxidant Peptide from Odorous Frog Skin." Protein & Peptide Letters 26, no. 3 (March 15, 2019): 160–69. http://dx.doi.org/10.2174/0929866525666181114153136.

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Background: Amphibian skin plays an essential role in protecting organisms from harmful external factors such as UV radiation. How amphibians protect themselves from reactive oxygen species following long-term sun exposure is an important and interesting question. Amphibian skins possess a novel antioxidant system composed of various Antioxidant Peptides (AOPs), which maintain redox homeostasis. However, only a few AOPs have been identified so far. Methods: Using combinational methods of peptidomics and genomics, we characterized a novel gene-encoded antioxidant peptide (herein named OA-VI12) from Odorrana andersonii skin secretions, which was produced by the post-translational processing of a 59-residue prepropeptide. The amino acid sequence of the OA-V112 was 'VIPFLACRPLGL', with a molecular mass of 1298.6 Da and no observed post-transcriptional modifications. Functional analysis demonstrated that OA-VI12 was capable of scavenging ABTS+, DPPH, NO and decreasing the Fe3+ production. Results: We determined that the C7 amino acid was responsible for ABTS+ and Fe3+ scavenging, activities, the F4, C7, and P9 amino acids were crucial for DPPH scavenging activity, and the P9 amino acid was responsible for NO scavenging activity. Unlike several other amphibian peptides, OA-VI12 did not accelerate wound healing in a full-thickness skin-wound mouse model and did not demonstrate direct microbial killing. Here, we identified and named a novel gene-encoded antioxidant peptide from the skin secretions of an odorous frog species, which may assist in the development of potential antioxidant candidates. Conclusion: This study may help improve our understanding of the molecular basis of amphibians’ adaptation to environments experiencing long-term UV radiation.

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Patocka, Jiri, Eugenie Nepovimova, Blanka Klimova, Qinghua Wu, and Kamil Kuca. "Antimicrobial Peptides: Amphibian Host Defense Peptides." Current Medicinal Chemistry 26, no. 32 (November 19, 2019): 5924–46. http://dx.doi.org/10.2174/0929867325666180713125314.

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Antimicrobial Peptides (AMPs) are one of the most common components of the innate immune system that protect multicellular organisms against microbial invasion. The vast majority of AMPs are isolated from the frog skin. Anuran (frogs and toads) skin contains abundant AMPs that can be developed therapeutically. Such peptides are a unique but diverse group of molecules. In general, more than 50% of the amino acid residues form the hydrophobic part of the molecule. Normally, there are no conserved structural motifs responsible for activity, although the vast majority of the AMPs are cationic due to the presence of multiple lysine residues; this cationicity has a close relationship with antibacterial activity. Notably, recent evidence suggests that synthesis of AMPs in frog skin may confer an advantage on a particular species, although they are not essential for survival. Frog skin AMPs exert potent activity against antibiotic-resistant bacteria, protozoa, yeasts, and fungi by permeating and destroying the plasma membrane and inactivating intracellular targets. Importantly, since they do not bind to a specific receptor, AMPs are less likely to induce resistance mechanisms. Currently, the best known amphibian AMPs are esculentins, brevinins, ranacyclins, ranatuerins, nigrocin-2, magainins, dermaseptins, bombinins, temporins, and japonicins-1 and -2, and palustrin-2. This review focuses on these frog skin AMPs and the mechanisms underlying their antimicrobial activity. We hope that this review will provide further information that will facilitate further study of AMPs and cast new light on novel and safer microbicides.

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McMillan, Katelyn A. M., and Melanie R. Power Coombs. "Review: Examining the Natural Role of Amphibian Antimicrobial Peptide Magainin." Molecules 25, no. 22 (November 20, 2020): 5436. http://dx.doi.org/10.3390/molecules25225436.

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Host defense peptides (HDPs) are a group of antimicrobial peptides (AMPs) that are crucial components of the innate immune system of many different organisms. These small peptides actively kill microbes and prevent infection. Despite the presence of AMPs in the amphibian immune system, populations of these organisms are in decline globally. Magainin is an AMP derived from the African clawed frog (Xenopus laevis) and has displayed potent antimicrobial effects against a wide variety of microbes. Included in this group of microbes are known pathogens of the African clawed frog and other amphibian species. Arguably, the most deleterious amphibious pathogen is Batrachochytrium dendrobatidis, a chytrid fungus. Investigating the mechanism of action of magainin can help understand how to effectively fight off infection. By understanding amphibian AMPs’ role in the frog, a potential conservation strategy can be developed for other species of amphibians that are susceptible to infections, such as the North American green frog (Rana clamitans). Considering that population declines of these organisms are occurring globally, this effort is crucial to protect not only these organisms but the ecosystems they inhabit as well.

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Holthausen, David J., Sanil George, and Joshy Jacob. "Amphibian innate immune mediators protect against human Influenza strains." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 63.7. http://dx.doi.org/10.4049/jimmunol.196.supp.63.7.

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Abstract Frogs and toads are incredible reservoirs of biologically active peptides. Amphibians secrete host defense peptides from their skin as part of their innate immune response. This ancient response acts to protect the amphibians against microbes. The quantity and scope of these secreted peptides dwarfs mammalian analogues, accounting for a substantial portion of all known host defense peptides. The non-invasive and non-harmful methods for frog peptide collection, in tandem with the abundance and breadth of these peptides, makes them excellent choices for novel peptide drug therapies. Studies have shown that these peptides can effectively neutralize enveloped viruses, mycobacteria, gram-negative and gram-positive bacteria, fungi, and even cancerous or transformed cells. Because of the nature of antimicrobial peptides, often targeting the most critical, conserved aspects of a micro-organism, they may prove a vital alternative to conventional drugs plagued by pathogen resistance. Given this untapped potential for anti-viral therapies, we assessed novel host defense peptides from the skin of the Indian fungoid frog, Hylarana malabarica. During our analysis, we isolated several peptides from H. malabarica that show anti-viral activity against human influenza viruses. Our studies indicate that peptides from H. malabarica demonstrate anti-influenza activity in vitro, and also show potential as an anti-viral therapy in vivo.

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Yang, Jie, Chengliang Tong, Junmei Qi, Xiaoying Liao, Xiaokun Li, Xu Zhang, Mei Zhou, et al. "Engineering and Structural Insights of a Novel BBI-like Protease Inhibitor Livisin from the Frog Skin Secretion." Toxins 14, no. 4 (April 12, 2022): 273. http://dx.doi.org/10.3390/toxins14040273.

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The Bowman–Birk protease inhibitor (BBI) family is a prototype group found mainly in plants, particularly grasses and legumes, which have been subjected to decades of study. Recently, the discovery of attenuated peptides containing the canonical Bowman–Birk protease inhibitory motif has been detected in the skin secretions of amphibians, mainly from Ranidae family members. The roles of these peptides in amphibian defense have been proposed to work cooperatively with antimicrobial peptides and reduce peptide degradation. A novel trypsin inhibitory peptide, named livisin, was found in the skin secretion of the green cascade frog, Odorrana livida. The cDNA encoding the precursor of livisin was cloned, and the predicted mature peptide was characterized. The mature peptide was found to act as a potent inhibitor against several serine proteases. A comparative activity study among the native peptide and its engineered analogs was performed, and the influence of the P1 and P2′ positions, as well as the C-terminal amidation on the structure–activity relationship for livisin, was illustrated. The findings demonstrated that livisin might serve as a potential drug discovery/development tool.

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Ramsey, Jeremy P., Laura K. Reinert, Laura K. Harper, Douglas C. Woodhams, and Louise A. Rollins-Smith. "Immune Defenses against Batrachochytrium dendrobatidis, a Fungus Linked to Global Amphibian Declines, in the South African Clawed Frog, Xenopus laevis." Infection and Immunity 78, no. 9 (June 28, 2010): 3981–92. http://dx.doi.org/10.1128/iai.00402-10.

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ABSTRACT Batrachochytrium dendrobatidis is a chytrid fungus that causes the lethal skin disease chytridiomycosis in amphibians. It is regarded as an emerging infectious disease affecting diverse amphibian populations in many parts of the world. Because there are few model amphibian species for immunological studies, little is known about immune defenses against B. dendrobatidis. We show here that the South African clawed frog, Xenopus laevis, is a suitable model for investigating immunity to this pathogen. After an experimental exposure, a mild infection developed over 20 to 30 days and declined by 45 days postexposure. Either purified antimicrobial peptides or mixtures of peptides in the skin mucus inhibited B. dendrobatidis growth in vitro. Skin peptide secretion was maximally induced by injection of norepinephrine, and this treatment resulted in sustained skin peptide depletion and increased susceptibility to infection. Sublethal X-irradiation of frogs decreased leukocyte numbers in the spleen and resulted in greater susceptibility to infection. Immunization against B. dendrobatidis induced elevated pathogen-specific IgM and IgY serum antibodies. Mucus secretions from X. laevis previously exposed to B. dendrobatidis contained significant amounts of IgM, IgY, and IgX antibodies that bind to B. dendrobatidis. These data strongly suggest that both innate and adaptive immune defenses are involved in the resistance of X. laevis to lethal B. dendrobatidis infections.

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VanCompernolle, Scott E., R. Jeffery Taylor, Kyra Oswald-Richter, Jiyang Jiang, Bryan E. Youree, John H. Bowie, Michael J. Tyler, et al. "Antimicrobial Peptides from Amphibian Skin Potently Inhibit Human Immunodeficiency Virus Infection and Transfer of Virus from Dendritic Cells to T Cells." Journal of Virology 79, no. 18 (September 15, 2005): 11598–606. http://dx.doi.org/10.1128/jvi.79.18.11598-11606.2005.

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ABSTRACT Topical antimicrobicides hold great promise in reducing human immunodeficiency virus (HIV) transmission. Amphibian skin provides a rich source of broad-spectrum antimicrobial peptides including some that have antiviral activity. We tested 14 peptides derived from diverse amphibian species for the capacity to inhibit HIV infection. Three peptides (caerin 1.1, caerin 1.9, and maculatin 1.1) completely inhibited HIV infection of T cells within minutes of exposure to virus at concentrations that were not toxic to target cells. These peptides also suppressed infection by murine leukemia virus but not by reovirus, a structurally unrelated nonenveloped virus. Preincubation with peptides prevented viral fusion to target cells and disrupted the HIV envelope. Remarkably, these amphibian peptides also were highly effective in inhibiting the transfer of HIV by dendritic cells (DCs) to T cells, even when DCs were transiently exposed to peptides 8 h after virus capture. These data suggest that amphibian-derived peptides can access DC-sequestered HIV and destroy the virus before it can be transferred to T cells. Thus, amphibian-derived antimicrobial peptides show promise as topical inhibitors of mucosal HIV transmission and provide novel tools to understand the complex biology of HIV capture by DCs.

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10

Xiao, Yao, Cunbao Liu, and Ren Lai. "Antimicrobial peptides from amphibians." BioMolecular Concepts 2, no. 1-2 (April 1, 2011): 27–38. http://dx.doi.org/10.1515/bmc.2011.006.

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AbstractIncreased prevalence of multi-drug resistance in pathogens has encouraged researchers to focus on finding novel forms of anti-infective agents. Antimicrobial peptides (AMPs) found in animal secretions are components of host innate immune response and have survived eons of pathogen evolution. Thus, they are likely to be active against pathogens and even those that are resistant to conventional drugs. Many peptides have been isolated and shown to be effective against multi-drug resistant pathogens. More than 500 AMPs have been identified from amphibians. The abundance of AMPs in frog skin is remarkable and constitutes a rich source for design of novel pharmaceutical molecules. Expression and post-translational modifications, discovery, activities and probable therapeutic application prospects of amphibian AMPs will be discussed in this article.

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Gaudino, G., A. Fasolo, G. Merlo, L. H. Lazarus, T. Renda, L. D'Este, and F. Vandesande. "Active peptides from amphibian skin are also amphibian neuropeptides." Peptides 6 (January 1985): 209–13. http://dx.doi.org/10.1016/0196-9781(85)90376-6.

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Zhou, Xiao Li, Xiao Xiao Meng, Qing Wang, Yi Ming Zhou, and Zong Jie Li. "Comparative Anti-Tumor Activity Study of Tartary Buckwheat Flavonoids and Amphibian Peptides." Advanced Materials Research 781-784 (September 2013): 1270–74. http://dx.doi.org/10.4028/www.scientific.net/amr.781-784.1270.

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In China, many kinds of natural products extracted from plant and animal were used to treat cancer. Flavonoids extracted from tartary buckwheat and skin peptide purified from rufous-spotted torrent frog had respectively been proved to have anti-tumor activity. In present study, both tartary buckwheat flavonoids and amphibian frog peptides were applied for cell proliferation inhibitory activity against human gastric cancer MGC 80-3 cells using MTT assay. According to the data, the buckwheat flavonoids exhibited much stronger anti-tumor activity than amphibian peptides, and the complex mixture of this two kinds of bioactive compounds still possess anti-tumor activity.

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Negri, Lucia, Pietro Melchiorri, and Roberta Lattanzi. "Pharmacology of Amphibian Opiate Peptides." Peptides 21, no. 11 (November 2000): 1639–47. http://dx.doi.org/10.1016/s0196-9781(00)00295-3.

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Mangoni, Maria Luisa. "Preface to Amphibian Antimicrobial Peptides." Biochimica et Biophysica Acta (BBA) - Biomembranes 1788, no. 8 (August 2009): 1535–36. http://dx.doi.org/10.1016/j.bbamem.2009.05.016.

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Bowie, John H., Kate L. Wegener, Brian C. S. Chia, Paul A. Wabnitz, John A. Carver, Michael J. Tyler, and John C. Wallace. "Host Defence Antibacterial Peptides from Skin Secretions of Australian Amphibians. The Relationship Between Structure and Activity." Protein & Peptide Letters 6, no. 5 (October 1999): 259–69. http://dx.doi.org/10.2174/092986650605221117113359.

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Abstract: Peptides have been isolated and characterised from the secretions of skin glands of twenty five species of Australian amphibian. Many peptides are host defence agents, showing, for example, neuropeptide and/or antibacterial activity. This review describes the relationship between activity and structure of the antibacterial peptides, particularly the caerin and uperin groups of peptide from the genera Litoria and Uperoleia.

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Rollins-Smith, Louise A. "The role of amphibian antimicrobial peptides in protection of amphibians from pathogens linked to global amphibian declines." Biochimica et Biophysica Acta (BBA) - Biomembranes 1788, no. 8 (August 2009): 1593–99. http://dx.doi.org/10.1016/j.bbamem.2009.03.008.

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Demori, Ilaria, Zeinab El Rashed, Giulia De Negri Atanasio, Alice Parodi, Enrico Millo, Annalisa Salis, Andrea Costa, et al. "First Evidence of Anti-Steatotic Action of Macrotympanain A1, an Amphibian Skin Peptide from Odorrana macrotympana." Molecules 27, no. 21 (November 1, 2022): 7417. http://dx.doi.org/10.3390/molecules27217417.

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Many different amphibian skin peptides have been characterized and proven to exert various biological actions, such as wound-healing, immunomodulatory, anti-oxidant, anti-inflammatory and anti-diabetic effects. In this work, the possible anti-steatotic effect of macrotympanain A1 (MA1) (FLPGLECVW), a skin peptide isolated from the Chinese odorous frog Odorrana macrotympana, was investigated. We used a well-established in vitro model of hepatic steatosis, consisting of lipid-loaded rat hepatoma FaO cells. In this model, a 24 h treatment with 10 µg/mL MA1 exerted a significant anti-steatotic action, being able to reduce intracellular triglyceride content. Accordingly, the number and diameter of cytosolic lipid droplets (LDs) were reduced by peptide treatment. The expression of key genes of hepatic lipid metabolism, such as PPARs and PLINs, was measured by real-time qPCR. MA1 counteracted the fatty acid-induced upregulation of PPARγ expression and increased PLIN3 expression, suggesting a role in promoting lipophagy. The present data demonstrate for the first time a direct anti-steatotic effect of a peptide from amphibian skin secretion and pave the way to further studies on the use of amphibian peptides for beneficial actions against metabolic diseases.

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Moore, K. S., C. L. Bevins, N. Tomassini, K. M. Huttner, K. Sadler, J. E. Moreira, J. Reynolds, and M. Zasloff. "A novel peptide-producing cell in Xenopus: multinucleated gastric mucosal cell strikingly similar to the granular gland of the skin." Journal of Histochemistry & Cytochemistry 40, no. 3 (March 1992): 367–78. http://dx.doi.org/10.1177/40.3.1552176.

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We have characterized a novel peptide-containing cell within the gastric mucosa of Xenopus laevis. The cell is a spherical, multinucleated syncytial structure containing a cytoplasmic space filled with dense rice-shaped granules, and is strikingly similar in morphology to the well-studied granular gland of the amphibian skin. Immunohistochemical and immunogold methods were used to demonstrate that several peptides previously isolated from the granular glands of the skin, including the antimicrobial peptides magainin and PGLa (a peptide with amino-terminal glycine and carboxy-terminal leucinamide), are also stored in granules present in these enteric cells. These data demonstrate that this enteric peptide-producing cell is strikingly similar both morphologically and biochemically to the granular gland, previously considered a highly specialized structure of the amphibian integument. This novel gastric mucosal cell, which we have designated a "granular multinucleated cell," is distinct in its morphology and its diversity of stored peptide products from other well-characterized peptide-containing cells in the vertebrate gastrointestinal tract.

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Soltaninejad, Hossein, Hadi Zare-Zardini, Mahtab Ordooei, Yaser Ghelmani, Akram Ghadiri-Anari, Sanaz Mojahedi, and Amir Ali Hamidieh. "Antimicrobial Peptides from Amphibian Innate Immune System as Potent Antidiabetic Agents: A Literature Review and Bioinformatics Analysis." Journal of Diabetes Research 2021 (June 29, 2021): 1–10. http://dx.doi.org/10.1155/2021/2894722.

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Antimicrobial peptides, as an important member of the innate immune system, have various biological activities in addition to antimicrobial activity. There are some AMPs with antidiabetic activity, especially those isolated from amphibians. These peptides can induce insulin release via different mechanisms based on peptide type. In this review study, we collected all reported AMPs with antidiabetic activity. We also analyze the sequence and structure of these peptides for evaluation of sequence and structure effect on their antidiabetic activity. Based on this review, the biggest peptide family with antidiabetic activity is temporins with nine antidiabetic peptides. Frogs are the most abundant source of antidiabetic peptides. Bioinformatics analysis showed that an increase of positive net charge and a decrease of hydrophobicity can improve the insulinotropic effect of peptides. Peptides with higher positive net charge and Boman index showed higher activity. Based on this review article, AMPs with antidiabetic activity, especially those isolated from amphibians, can be used as novel antidiabetic drug for type 2 diabetes disease. So, amphibians are potential sources for active peptides which merit further evaluation as novel insulin secretagogues. However, strategy for the increase of stability and positive activity as well as the decrease of negative side effects must be considered.

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Demori, Ilaria, Zeinab El Rashed, Viola Corradino, Annamaria Catalano, Leila Rovegno, Linda Queirolo, Sebastiano Salvidio, et al. "Peptides for Skin Protection and Healing in Amphibians." Molecules 24, no. 2 (January 18, 2019): 347. http://dx.doi.org/10.3390/molecules24020347.

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Amphibian skin is not to be considered a mere tegument; it has a multitude of functions related to respiration, osmoregulation, and thermoregulation, thus allowing the individuals to survive and thrive in the terrestrial environment. Moreover, amphibian skin secretions are enriched with several peptides, which defend the skin from environmental and pathogenic insults and exert many other biological effects. In this work, the beneficial effects of amphibian skin peptides are reviewed, in particular their role in speeding up wound healing and in protection from oxidative stress and UV irradiation. A better understanding of why some species seem to resist several environmental insults can help to limit the ongoing amphibian decline through the development of appropriate strategies, particularly against pathologies such as viral and fungal infections.

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Bradford, AM, MJ Raftery, JH Bowie, JC Wallace, and MJ Tyler. "Peptides From Australian Frogs. The Structures of the Dynastins From Limnodynastes salmini and Fletcherin From Limnodynastes fletcheri." Australian Journal of Chemistry 46, no. 8 (1993): 1235. http://dx.doi.org/10.1071/ch9931235.

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The dermal glandular extracts of the Australian frog Limnodynastes salmini contain a number of peptides of the dynastin family. The related species Limnodynastes fletcheri contains only one peptide in its glandular extract; this compound, which we have named fletcherin, is unusual amongst amphibian peptides in that the N-terminal group corresponds to Ala. The primary structures of the dynastins and fletcherin are described.

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Conlon, J. Michael. "Clinical Applications of Amphibian Antimicrobial Peptides." Journal of Medical Sciences 4, no. 2 (June 17, 2011): 62–72. http://dx.doi.org/10.2174/1996327001104020062.

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Buchan, Alison M. J. "Regulatory peptides in the amphibian pancreas." Canadian Journal of Zoology 63, no. 9 (September 1, 1985): 2121–24. http://dx.doi.org/10.1139/z85-312.

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The pancreas from 11 amphibian species was investigated by immunocytochemical methods for the presence of immunoreactivity to a number of antisera raised to mammalian regulatory peptides. The hormones studied were insulin, pancreatic glucagon, enteroglucagon (glicentin), pancreatic polypeptide, somatostatin, gastrin, gastric inhibitory polypeptide, substance P, bombesin, methionine enkephalin, and vasoactive intestinal polypeptide. Immunoreactive cells were detected in all species with the antisera to insulin, somatostatin, pancreatic glucagon, enteroglucagon, and pancreatic polypeptide. The cells stained by the two glucagon antisera and the pancreatic polypeptide antiserum were identical in all species examined. Fine nerve fibres immunoreactive with the antiserum to vasoactive intestinal polypeptide were demonstrable only in the anuran species Hyla arborea (Hylidae). The remainder of the antisera did not detect either endocrine cells or nerve fibres in the species studied.

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Motta, Marcella. "Neuroendocrine effects of some amphibian peptides." Peptides 6 (January 1985): 131–35. http://dx.doi.org/10.1016/0196-9781(85)90363-8.

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Reshmy, V., V. Preeji, A. Parvin, K. Santhoshkumar, and S. George. "Molecular Cloning of a Novel Bradykinin-Related Peptide from the Skin of Indian Bronzed Frog Hylarana Temporalis." Genomics Insights 3 (January 2010): GEI.S5409. http://dx.doi.org/10.4137/gei.s5409.

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Bradykinin-related peptides (BRPs) constitute one of the most studied groups of bioactive peptides in amphibian skin secretions. The present study describes the successful isolation of a novel BRP (hylaranakinin TE) from the skin secretion of the Indian bronzed frog Hylarana temporalis. The deduced open reading frame consisted of 115 amino acid residues with a putative signal peptide of 22 amino acid residues, followed by a spacer region and mature peptide regions that encode for two BRPs: a canonical bradykinin R-9-R with a C-terminal extension of FVPASSL and Thr 6 -BK. The Thr 6 -BK reported in the present study had an unusual FP-insertion in the N-terminal part and ended in FAPEII, which is very different from the IAPAIV sequence reported in other ranid frogs. Unlike the mammalian bradykinin and its precursor, amphibian BRPs and their precursors are extremely variable, as evident from the present study. This forms the first report of BRPs from Hylarana temporalis, endemic to India and Sri Lanka.

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Wang, Guangshun, Karen M. Watson, Alan Peterkofsky, and Robert W. Buckheit. "Identification of Novel Human Immunodeficiency Virus Type 1-Inhibitory Peptides Based on the Antimicrobial Peptide Database." Antimicrobial Agents and Chemotherapy 54, no. 3 (January 19, 2010): 1343–46. http://dx.doi.org/10.1128/aac.01448-09.

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ABSTRACT To identify novel anti-HIV-1 peptides based on the antimicrobial peptide database (APD; http://aps.unmc.edu/AP/main.php ), we have screened 30 candidates and found 11 peptides with 50% effective concentrations (EC50) of <10 μM and therapeutic indices (TI) of up to 17. Furthermore, among the eight peptides (with identical amino acid compositions but different sequences) generated by shuffling the sequence of an aurein 1.2 analog, two had a TI twice that of the original sequence. Because antiviral peptides in the database have an arginine/lysine (R/K) ratio of >1, increases in the Arg contents of amphibian maximin H5 and dermaseptin S9 peptides and the database-derived GLK-19 peptide improved the TIs. These examples demonstrate that the APD is a rich resource and a useful tool for developing novel HIV-1-inhibitory peptides.

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Fu, Siqi, Canwei Du, Qijian Zhang, Jiayu Liu, Xushuang Zhang, and Meichun Deng. "A Novel Peptide from Polypedates megacephalus Promotes Wound Healing in Mice." Toxins 14, no. 11 (November 2, 2022): 753. http://dx.doi.org/10.3390/toxins14110753.

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Amphibian skin contains wound-healing peptides, antimicrobial peptides, and insulin-releasing peptides, which give their skin a strong regeneration ability to adapt to a complex and harsh living environment. In the current research, a novel wound-healing promoting peptide, PM-7, was identified from the skin secretions of Polypedates megacephalus, which has an amino acid sequence of FLNWRRILFLKVVR and shares no structural similarity with any peptides described before. It displays the activity of promoting wound healing in mice. Moreover, PM-7 exhibits the function of enhancing proliferation and migration in HUVEC and HSF cells by affecting the MAPK signaling pathway. Considering its favorable traits as a novel peptide that significantly promotes wound healing, PM-7 can be a potential candidate in the development of novel wound-repairing drugs.

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Erspamer, Vittorio. "The opioid peptides of the amphibian skin." International Journal of Developmental Neuroscience 10, no. 1 (February 1992): 3–30. http://dx.doi.org/10.1016/0736-5748(92)90003-i.

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Siano, Alvaro, Maria Humpola, Eliandre de Oliveira, Fernando Albericio, Arturo Simonetta, Rafael Lajmanovich, and Georgina Tonarelli. "Leptodactylus latrans Amphibian Skin Secretions as a Novel Source for the Isolation of Antibacterial Peptides." Molecules 23, no. 11 (November 11, 2018): 2943. http://dx.doi.org/10.3390/molecules23112943.

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Amphibians´ skin produces a diverse array of antimicrobial peptides that play a crucial role as the first line of defense against microbial invasion. Despite the immense richness of wild amphibians in Argentina, current knowledge about the presence of peptides with antimicrobial properties is limited to a only few species. Here we used LC-MS-MS to identify antimicrobial peptides with masses ranging from 1000 to 4000 Da from samples of skin secretions of Leptodactylus latrans (Anura: Leptodactylidae). Three novel amino acid sequences were selected for chemical synthesis and further studies. The three synthetic peptides, named P1-Ll-1577, P2-Ll-1298, and P3-Ll-2085, inhibited the growth of two ATCC strains, namely Escherichia coli and Staphylococcus aureus. P3-Ll-2085 was the most active peptide. In the presence of trifluoroethanol (TFE) and anionic liposomes, it adopted an amphipathic α-helical structure. P2-Ll-1298 showed slightly lower activity than P3-Ll-2085. Comparison of the MIC values of these two peptides revealed that the addition of seven amino acid residues (GLLDFLK) on the N-terminal of P2-Ll-1298 significantly improved activity against both strains. P1-Ll-1577, which remarkably is an anionic peptide, showed interesting antimicrobial activity against E. coli and S. aureus strain, showing marked membrane selectivity and non-hemolysis. Due to this, P1-L1-1577 emerges as a potential candidate for the development of new antibacterial drugs.

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Rollins-Smith, Louise A., Cynthia Carey, J. Michael Conlon, Laura K. Reinert, Jennifer K. Doersam, Tomas Bergman, Jerzy Silberring, Hilkka Lankinen, and David Wade. "Activities of Temporin Family Peptides against the Chytrid Fungus (Batrachochytrium dendrobatidis) Associated with Global Amphibian Declines." Antimicrobial Agents and Chemotherapy 47, no. 3 (March 2003): 1157–60. http://dx.doi.org/10.1128/aac.47.3.1157-1160.2003.

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ABSTRACT Temporin A and structurally related peptides produced in amphibian dermal granular glands and in wasp venom were tested for growth inhibition of Batrachochytrium dendrobatidis, a pathogen associated with global amphibian declines. Two natural amphibian temporins, a wasp temporin, and six synthetic analogs effectively inhibited growth. Differences in potency due to amino acid substitution suggest that ability to penetrate membranes and form an α-helical structure is important for their effectiveness against this pathogen.

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Chianese, Annalisa, Carla Zannella, Alessandra Monti, Anna De Filippis, Nunzianna Doti, Gianluigi Franci, and Massimiliano Galdiero. "The Broad-Spectrum Antiviral Potential of the Amphibian Peptide AR-23." International Journal of Molecular Sciences 23, no. 2 (January 14, 2022): 883. http://dx.doi.org/10.3390/ijms23020883.

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Viral infections represent a serious threat to the world population and are becoming more frequent. The search and identification of broad-spectrum antiviral molecules is necessary to ensure new therapeutic options, since there is a limited availability of effective antiviral drugs able to eradicate viral infections, and consequently due to the increase of strains that are resistant to the most used drugs. Recently, several studies on antimicrobial peptides identified them as promising antiviral agents. In detail, amphibian skin secretions serve as a rich source of natural antimicrobial peptides. Their antibacterial and antifungal activities have been widely reported, but their exploitation as potential antiviral agents have yet to be fully investigated. In the present study, the antiviral activity of the peptide derived from the secretion of Rana tagoi, named AR-23, was evaluated against both DNA and RNA viruses, with or without envelope. Different assays were performed to identify in which step of the infectious cycle the peptide could act. AR-23 exhibited a greater inhibitory activity in the early stages of infection against both DNA (HSV-1) and RNA (MeV, HPIV-2, HCoV-229E, and SARS-CoV-2) enveloped viruses and, on the contrary, it was inactive against naked viruses (PV-1). Altogether, the results indicated AR-23 as a peptide with potential therapeutic effects against a wide variety of human viruses.

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Barra, Donatella, and Maurizio Simmaco. "Amphibian skin: A promising resource for antimicrobial peptides." Trends in Biotechnology 13, no. 6 (June 1995): 205–9. http://dx.doi.org/10.1016/s0167-7799(00)88947-7.

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Pimenta, Daniel. "The amphibian skin secretion: beyond the antimicrobial peptides." Toxicon 168 (October 2019): S7. http://dx.doi.org/10.1016/j.toxicon.2019.06.050.

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de Magistris, L., B. Annibale, G. Delle Fave, M. Salera, M. Puoti, E. Giordano, A. Forte, and V. Erspamer. "Peptides of the APUD system in amphibian skins." Peptides 6 (January 1985): 203–8. http://dx.doi.org/10.1016/0196-9781(85)90375-4.

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Kreil, Günther. "Hormone, opioid and other peptides from amphibian skin." Regulatory Peptides 40, no. 2 (July 1992): 188. http://dx.doi.org/10.1016/0167-0115(92)90294-5.

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Rivas, Luis, Juan Román Luque-Ortega, and David Andreu. "Amphibian antimicrobial peptides and Protozoa: Lessons from parasites." Biochimica et Biophysica Acta (BBA) - Biomembranes 1788, no. 8 (August 2009): 1570–81. http://dx.doi.org/10.1016/j.bbamem.2008.11.002.

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Doyle, Jason, Lyndon E. Llewellyn, Craig S. Brinkworth, John H. Bowie, Kate L. Wegener, Tomas Rozek, Paul A. Wabnitz, John C. Wallace, and Michael J. Tyler. "Amphibian peptides that inhibit neuronal nitric oxide synthase." European Journal of Biochemistry 269, no. 1 (January 2002): 100–109. http://dx.doi.org/10.1046/j.0014-2956.2002.02630.x.

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Negri, L., L. Noviello, and V. Noviello. "Central Effects of Amphibian Opioid Peptides in Rats." Pharmacological Research 27 (May 1993): 43–44. http://dx.doi.org/10.1006/phrs.1993.1056.

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Quassinti, Luana, Ennio Maccari, Oretta Murri, and Massimo Bramucci. "Synthetic seminal plasma peptide inhibits testosterone production in frog testis in vitro." Reproduction, Fertility and Development 19, no. 2 (2007): 398. http://dx.doi.org/10.1071/rd06044.

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The role of synthetic seminal plasma peptide, designed using biochemical and mass spectroscopy analyses of native peptides extracted from seminal plasma, was studied in amphibian (Rana esculenta) testicular steroidogenesis. Production of testosterone and prostaglandin F2α was determined by incubating frog testes with synthetic peptide in vitro. Analysis of the data showed a dose-dependent inhibition of testosterone production (43% at 10−5 m concentration) without prostaglandin F2α synthesis being affected. Determination of the peptide activity during the annual R. esculenta reproductive cycle showed inhibition of testosterone production in post-reproductive and recovery periods, suggesting a possible involvement of peptide in gonad steroidogenesis.

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Bina Perl, R. G., Sarig Gafny, Yoram Malka, Sharon Renan, Douglas C. Woodhams, Louise Rollins-Smith, James D. Pask, Molly C. Bletz, Eli Geffen, and Miguel Vences. "Natural history and conservation of the rediscovered Hula painted frog, Latonia nigriventer." Contributions to Zoology 86, no. 1 (February 13, 2017): 11–37. http://dx.doi.org/10.1163/18759866-08601002.

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Dramatic global amphibian declines have recently led to an increased concern for many species of this animal class. The enigmatic Hula painted frog (Latonia nigriventer), the first amphibian to be declared extinct but unexpectedly rediscovered in 2011, has remained one of the rarest and most poorly understood amphibians worldwide. Gathering basic biological information on this species, along with an understanding of its disease-related threats remains fundamental for developing risk assessments and conservation strategies. Our surveys in recent years confirmed that L. nigriventer is a localised species with elusive habits. The species appears to follow an opportunistic breeding phenology and has a tadpole morphology similar to its well-studied sister group Discoglossus. However, the adults’ extended annual presence in the aquatic habitat is a major difference from species of Discoglossus. We detected the amphibian chytrid fungus, Batrachochytrium dendrobatidis (Bd), in northern Israel and on Hula painted frogs but did not observe any signs of chytridiomycosis in this species. Our preliminary data on aspects of the innate immunity of L. nigriventer suggest that the skin mucosome of this species contains antimicrobial peptides and a bacterial community differing from other syntopic frogs (Pelophylax bedriagae). The combined knowledge of both natural history and innate immunity of L. nigriventer provides valuable insights to direct future research and conservation management of this critically endangered frog species.

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Bai, Bing, Xiaojuan Hou, Lei Wang, Lilin Ge, Yu Luo, Chengbang Ma, Mei Zhou, Jinao Duan, Tianbao Chen, and Chris Shaw. "Feleucins: Novel Bombinin Precursor-Encoded Nonapeptide Amides from the Skin Secretion ofBombina variegata." BioMed Research International 2014 (2014): 1–8. http://dx.doi.org/10.1155/2014/671362.

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The first amphibian skin antimicrobial peptide (AMP) to be identified was named bombinin, reflecting its origin from the skin of the European yellow-bellied toad (Bombina variegata). Bombinins and their related peptides, the bombinin Hs, were subsequently reported from other bombinid toads. Molecular cloning of bombinin-encoding cDNAs from skin found that bombinins and bombinin Hs were coencoded on the same precursor proteins. Here, we report the molecular cloning of two novel cDNAs from a skin secretion-derived cDNA library ofB. variegatawhose open-reading frames each encode a novel bombinin (GIGGALLNVGKVALKGLAKGLAEHFANamide) and a C-terminally located single copy of a novel nonapeptide (FLGLLGGLLamide or FLGLIGSLLamide). These novel nonapeptides were named feleucin-BV1 and feleucin-BV2, respectively. The novel bombinin exhibited 89% identity to homologues from the toads,B. microdeladigitoraandB. maxima. The feleucins exhibited no identity with any amphibian AMP archived in databases. Synthetic feleucins exhibited a weak activity againstStaphylococcus aureus(128–256 mg/L) but feleucin-BV1 exhibited a synergistic action with the novel bombinin. The present report clearly demonstrates that the skin secretions of bombinid toads continue to represent a source of peptides of novel structure that could provide templates for the design of therapeutics.

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Darribère, T., K. Guida, H. Larjava, K. E. Johnson, K. M. Yamada, J. P. Thiery, and J. C. Boucaut. "In vivo analyses of integrin beta 1 subunit function in fibronectin matrix assembly." Journal of Cell Biology 110, no. 5 (May 1, 1990): 1813–23. http://dx.doi.org/10.1083/jcb.110.5.1813.

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Early development of the urodele amphibian Pleurodeles waltl is accompanied by a process of progressive fibronectin (FN) fibrillogenesis. FN begins to assemble into fibrils on the inner surface of the blastocoele roof at the early blastula stage and progressively forms a complex extracellular matrix. We have analyzed the mechanisms of FN-fibril formation under normal and experimental conditions in vivo with the following probes: iodinated FN, fluorescein-labeled FN, synthetic peptides containing the Arg-Gly-Asp (RGD) cell surface recognition sequence of FN, and polyclonal antibodies against both beta 1 subunit of the amphibian FN receptor and the cytoplasmic domain of beta 1 subunit. We report that in living embryos, exogenous labeled mammalian FN injected into the amphibian blastocoele undergoes FN-fibril formation in spatiotemporal patterns similar to those of endogenous FN. This indicates regulation of fibrillogenesis by the cell surface rather than by changes in the type of FN. Fibrillogenesis is inhibited in a dose-dependent manner both by the GRGDS peptide and monospecific antibodies to amphibian integrin beta 1 subunit. Furthermore, when injected intracellularly into uncleaved embryos or into selected blastomeres, antibodies to the cytoplasmic domain of integrin beta 1 subunit produce a reversible inhibition of FN-fibril formation that follows early cell lineages and cause delays in development. Together, these data indicate that in vivo, the integrin beta 1 subunit and the RGD recognition signal are essential for the proper assembly of FN fibrils in early amphibian development.

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Lin, Diana, Darcy Sutherland, Sambina Islam Aninta, Nathan Louie, Ka Ming Nip, Chenkai Li, Anat Yanai, et al. "Mining Amphibian and Insect Transcriptomes for Antimicrobial Peptide Sequences with rAMPage." Antibiotics 11, no. 7 (July 15, 2022): 952. http://dx.doi.org/10.3390/antibiotics11070952.

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Antibiotic resistance is a global health crisis increasing in prevalence every day. To combat this crisis, alternative antimicrobial therapeutics are urgently needed. Antimicrobial peptides (AMPs), a family of short defense proteins, are produced naturally by all organisms and hold great potential as effective alternatives to small molecule antibiotics. Here, we present rAMPage, a scalable bioinformatics discovery platform for identifying AMP sequences from RNA sequencing (RNA-seq) datasets. In our study, we demonstrate the utility and scalability of rAMPage, running it on 84 publicly available RNA-seq datasets from 75 amphibian and insect species—species known to have rich AMP repertoires. Across these datasets, we identified 1137 putative AMPs, 1024 of which were deemed novel by a homology search in cataloged AMPs in public databases. We selected 21 peptide sequences from this set for antimicrobial susceptibility testing against Escherichia coli and Staphylococcus aureus and observed that seven of them have high antimicrobial activity. Our study illustrates how in silico methods such as rAMPage can enable the fast and efficient discovery of novel antimicrobial peptides as an effective first step in the strenuous process of antimicrobial drug development.

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Proaño-Bolaños, Carolina, Ailín Blasco-Zúñiga, José Rafael Almeida, Lei Wang, Miguel Angel Llumiquinga, Miryan Rivera, Mei Zhou, Tianbao Chen, and Chris Shaw. "Unravelling the Skin Secretion Peptides of the Gliding Leaf Frog, Agalychnis spurrelli (Hylidae)." Biomolecules 9, no. 11 (October 30, 2019): 667. http://dx.doi.org/10.3390/biom9110667.

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Frog skin secretions contain medically-valuable molecules, which are useful for the discovery of new biopharmaceuticals. The peptide profile of the skin secretion of Agalychnis spurrelli has not been investigated; therefore, the structural and biological characterization of its compounds signify an inestimable opportunity to acquire new biologically-active chemical scaffolds. In this work, skin secretion from this amphibian was analysed by molecular cloning and tandem mass spectrometry. Although the extent of this work was not exhaustive, eleven skin secretion peptides belonging to five peptide families were identified. Among these, we report the occurrence of two phyllokinins, and one medusin-SP which were previously reported in other related species. In addition, eight novel peptides were identified, including four dermaseptins, DRS-SP2 to DRS-SP5, one phylloseptin-SP1, and three orphan peptides. Phylloseptin-SP1 and dermaseptins-SP2 were identified in HPLC fractions based on their molecular masses determined by MALDI-TOF MS. Among the antimicrobial peptides, dermaseptin-SP2 was the most potent, inhibiting Escherichia coli, Staphylococcus aureus, and ORSA with a minimum inhibitory concentration (MIC) of 2.68 μM, and Candida albicans with an MIC of 10.71 μM, without haemolytic effects. The peptides described in this study represent but a superficial glance at the considerable structural diversity of bioactive peptides produced in the skin secretion of A. spurrelli.

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Oskyrko, S., J. Dudkina, T. Nikolaieva, T. Halenova, and O. Marushchak. "Variability and properties of host defense peptides from the skin secretions of anurans." Bulletin of Taras Shevchenko National University of Kyiv. Series: Biology 76, no. 2 (2018): 51–56. http://dx.doi.org/10.17721/1728_2748.2018.76.51-56.

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Cationic antimicrobial proteins are an important part of innate nonspecific immunity. It is the first defensive level, which is inherent in almost all living organisms. The main objective of such proteins is the destruction of dangerous microorganisms (fungi, bacteria, viruses, parasites etc.). The skin of amphibians is a rich source of these molecules, which are produced and stockpiled in skin glands, which are usually located on the dorsal side of the body. Basically, they are spread over the surface of the body or grouped in special morphological structures – parotids. Currently the host defensive proteins were found in members of all families of amphibians, that suggests a connection among them with evolutionary advantages. Moreover, amphibian antimicrobial proteins can be used in modern medicine. Amphibians can become a rich source of biologically active agents and usage of them is very beneficial for pharmaceutical industry. These substances appeared to have much more abilities than it was believed before. For example, they can be used in methods of blood folding or antiviral therapy. Taking this into account, it is very promising to study antimicrobial proteins in Ukraine (from 15 anuran species of 5 families (Pelobatidae, Hylidae, Bufonidae, Ranidae and Bombinatoridae). This article describes the chemical structure and properties of the antimicrobial proteins presently known from the studies and their presence in different families of Anura. The main aim of the work is to show the variability of these substances in anurans to create a background for further investigations of amphibians' antimicrobial proteins in Ukraine and studying of their pharmaceutical potential.

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Rinaldi, Andrea C. "Antimicrobial peptides from amphibian skin: an expanding scenario: Commentary." Current Opinion in Chemical Biology 6, no. 6 (December 2002): 799–804. http://dx.doi.org/10.1016/s1367-5931(02)00401-5.

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Cei, J. M. "Taxonomic and evolutionary significance of peptides in amphibian skin." Peptides 6 (January 1985): 13–16. http://dx.doi.org/10.1016/0196-9781(85)90344-4.

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Pérez, L. O., N. L. Cancelarich, S. Aguilar, N. G. Basso, and M. M. Marani. "Genetic analysis of signal peptides in amphibian antimicrobial secretions." Journal of Genetics 97, no. 5 (November 7, 2018): 1205–12. http://dx.doi.org/10.1007/s12041-018-1018-5.

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Liu, Naixin, Zhe Li, Buliang Meng, Wenxin Bian, Xiaojie Li, Siyuan Wang, Xiaoqing Cao, et al. "Accelerated Wound Healing Induced by a Novel Amphibian Peptide (OA-FF10)." Protein & Peptide Letters 26, no. 4 (March 28, 2019): 261–70. http://dx.doi.org/10.2174/0929866526666190124144027.

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Background: Despite the continued development of modern medicine, chronic wounds are still a critical issue in clinical treatment, placing a great physiological, psychological, and financial burden on patients. Researchers have investigated many methods to solve this problem, with bioactive peptides gaining increasing attention due to their considerable advantages and diverse functions, as well as low cost, simple storage, and easy transportation. Methods: In this research, a novel peptide (named OA-FF10) was identified from the skin secretions of the odorous frog species Odorrana andersonii. The sequence of mature OA-FF10 was “FFTTSCRSGC”, which was produced by the post-translational processing of a 61-residue prepropeptide. Results: Similar to most frog peptides, OA-FF10 showed an intramolecular disulfide bridge at the C-terminus. OA-FF10 demonstrated no antibacterial, antioxidant, hemolytic, or acute toxic activity, but promoted wound healing and proliferation of human keratinocytes (HaCaT) both time- and dose-dependently. Furthermore, while OA-FF10 had no effect on wound healing of Human Skin Fibroblasts (HSF), it did accelerate healing in a full-thickness skin-wound mouse model. Conclusion: Our research revealed the strong wound-healing activity of OA-FF10 in vivo and in vitro, thus providing a new candidate for the development of novel wound-healing drugs.

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Kakar, Anant, Jeanett Holzknecht, Sandrine Dubrac, Maria Luisa Gelmi, Alessandra Romanelli, and Florentine Marx. "New Perspectives in the Antimicrobial Activity of the Amphibian Temporin B: Peptide Analogs Are Effective Inhibitors of Candida albicans Growth." Journal of Fungi 7, no. 6 (June 7, 2021): 457. http://dx.doi.org/10.3390/jof7060457.

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Temporin B (TB) is a short, positively charged peptide secreted by the granular glands of the European frog Rana temporaria. While the antibacterial and antiviral efficacy of TB and some of its improved analogs are well documented, nothing is known about their antifungal potency so far. We dedicated this study to characterize the antifungal potential of the TB analog TB_KKG6K and the newly designed D-Lys_TB_KKG6K, the latter having the L-lysines replaced by the chiral counterpart D-lysines to improve its proteolytic stability. Both peptides inhibited the growth of opportunistic human pathogenic yeasts and killed planktonic and sessile cells of the most prevalent human pathogen, Candida albicans. The anti-yeast efficacy of the peptides coincided with the induction of intracellular reactive oxygen species. Their thermal, cation, pH and serum tolerance were similar, while the proteolytic stability of D-Lys_TB_KKG6K was superior to that of its template peptide. Importantly, both peptides lacked hemolytic activity and showed minimal in vitro cytotoxicity in primary human keratinocytes. The tolerance of both peptides in a reconstructed human epidermis model further supports their potential for topical application. Our results open up an exciting field of research for new anti-Candida therapeutic options based on amphibian TB analogs.

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Journal articles on the topic 'Amphibian peptides'

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