Unravelling the Skin Secretion Peptides of the Gliding Leaf Frog, Agalychnis spurrelli (Hylidae) (original) (raw)
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Novel Antimicrobial Peptides Isolated from Skin Secretions of the Mexican Frog Hyla eximia
Protein and Peptide Letters, 2009
High-resolution mass spectrometry-based peptidomics has been used to characterize several components in electro-stimulated skin secretions of the endemic Mexican frog Pachymedusa dacnicolor. Peptide mass screening performed in an Orbitrap-XL mass spectrometer showed that P. dacnicolor skin secretions possess 194 different components with molecular masses ranging mainly from 500 to 6,000 Da. Dozens of molecules were partially sequenced including two novel protease inhibitors. Additionally, one posttranslationally modified bradykinin and two novel dermaseptin-like antimicrobial peptides were fully sequenced. The novel peptide named here DMS-DA5 was fully characterized and showed potent antibacterial activity against various bacteria such as Escherichia coli, Bacillus subtilis, Salmonella enterica serovar typhimurium, and Pseudomonas aeruginosa with minimal inhibitory concentrations from 3.10 to 25.0 lM.
Antimicrobial Peptides from Skin Secretions of Hypsiboas pulchellus (Anura: Hylidae)
Journal of Natural Products, 2014
The skin of many amphibians produces a large repertoire of antimicrobial peptides that are crucial in the first line of defense against microbial invasion. Despite the immense richness of wild amphibians in Argentina, knowledge about peptides with antimicrobial properties is limited to a few species. Here we used LC-MS-MS to analyze samples of Hypsiboas pulchellus skin with the aim to identify antimicrobial peptides in the mass range of 1000 to 2000 Da. Twenty-three novel sequences were identified by MS, three of which were selected for chemical synthesis and further studies. The three synthetic peptides, named P1- Hp-1971, P2-Hp-1935, and P3-Hp-1891, inhibited the growth of two ATCC strains: Escherichia coli (MIC: 16, 33, and 17 μM, respectively) and Staphylococcus aureus (MIC: 8, 66, and 17 μM, respectively). P1-Hp-1971 and P3-Hp-1891 were the most active peptides. P1-Hp-1971, which showed the highest therapeutic indices (40 for E. coli and 80 for S. aureus), is a proline-glycine-rich peptide with a highly unordered structure, while P3-Hp-1891 adopts an amphipathic α-helical structure in the presence of 2,2,2-trifluoroethanol and anionic liposomes. This is the first peptidomic study of Hypsiboas pulchellus skin secretions to allow the identification of antimicrobial peptides.
ANTIMICROBIAL PEPTIDES FROM ANURANS SKIN SECRETIONS
This article is an overview of antimicrobial peptides found in anurans skin secretions. These molecules constitute an initial barrier against microbial infections because of their activity against a large array of microorganisms. These peptides hold remarkable pharmaceutical and technological interest since they selectively kill microorganisms and are unlikely to induce resistance in pathogens. Also, outstanding synergism occurs when these peptides are combined with classic antibiotics and other antimicrobial peptides.
Toxicon : official journal of the International Society on Toxinology, 2007
Two peptides with differential cytolytic activity against bacteria, a fungus pathogenic to amphibians, and mammalian cells were isolated from norepinephrine-stimulated skin secretions of the Lemur leaf frog Hylomantis lemur Boulenger, 1882. Dermaseptin-L1 (GLWSKIKEAAKAAGKAALNAVTGLVNQGDQPS) was active against the Gram-negative bacterium Escherichia coli (MIC=8 microM) but inactive against the Gram-positive bacterium Staphylococcus aureus. This peptide inhibited growth of zoospores of the chytrid fungus Batrachochytrium dendrobatidis at concentrations above 25 microM but did not completely inhibit growth at 100 microM. Phylloseptin-L1 (LLGMIPLAISAISALSKL.NH2) was active against S. aureus (MIC=8 microM) but was inactive against E. coli. This peptide also inhibited growth of B. dendrobatidis zoospores at concentrations above 25 microM with complete inhibition at 100 microM. Dermaseptin-L1 showed selective cytolytic activity against HepG2 human hepatoma-derived cells (LC50=45 microM) com...
Frog's skin secretions are known to present peculiar characteristics involving an arsenal of bioactive molecules. These organisms, in response to stress, injury or predator attack, release a viscous toxic secretion through granular glands containing biogenic amines, alkaloids, steroids, proteins and also peptides. Among such compounds, the antimicrobial peptides (AMPs) are responsible to play an important role in amphibian first-line defense against pathogenic microorganisms such as Gram-negative and positive bacteria, fungi and virus. In amphibians, AMPs have been isolated from different species and functionally studied, presenting not only antimicrobial but also antitumor, antifungal, anti-protozoa and spermicidal activities. However, a large number of AMPs have also shown cytotoxic activities against mammalian cells. In order to develop novel anti-infective drugs with low side effects, recent research has also been done to describe novel frog AMPs with different structural patterns. In this context, this review will focus on the antimicrobial activities of nine recently discovered amphibian AMPs including phylloseptins, nigrocins, japonicins, palustrins, parkerins, jingdongins, medusins, limnonectins and hylaranins. The biochemical properties will be discussed, as well as their possible applications in human health as new alternatives to conventional medicines.
Amphibian Skin and Skin Secretion: An Exotic Source of Bioactive Peptides and Its Application
Foods
Amphibians have been consumed as an alternative protein source all around the world due to their delicacy. The skin of edible amphibians, particularly frogs and giant salamanders, always goes to waste without further utilization. However, these wastes can be utilized to extract protein and bioactive peptides (BPs). Various BPs have been extracted and reported for numerous biological activities such as antioxidant, antimicrobial, anticancer, antidiabetic, etc. The main BPs identified were brevinins, bombesins, dermaseptins, esculentins, magainin, temporins, tigerinins, and salamandrins. This review provides a comprehensive discussion on various BPs isolated and identified from different amphibian skins or skin secretion and their biological activities. The general nutritional composition and production statues of amphibians were described. Additionally, multiple constraints against the utilization of amphibian skin and secretions are reported. Finally, the prospective applications of...
2007
Two peptides with differential cytolytic activity against bacteria, a fungus pathogenic to amphibians, and mammalian cells were isolated from norepinephrine-stimulated skin secretions of the Lemur leaf frog Hylomantis lemur Boulenger, 1882. Dermaseptin-L1 (GLWSKIKEAAKAAGKAALNAVTGLVNQGDQPS) was active against the Gram-negative bacterium Escherichia coli (MIC ¼ 8 mM) but inactive against the Gram-positive bacterium Staphylococcus aureus. This peptide inhibited growth of zoospores of the chytrid fungus Batrachochytrium dendrobatidis at concentrations above 25 mM but did not completely inhibit growth at 100 mM. Phylloseptin-L1 (LLGMIPLAISAISALSKL.NH 2 ) was active against S. aureus (MIC ¼ 8 mM) but was inactive against E. coli. This peptide also inhibited growth of B. dendrobatidis zoospores at concentrations above 25 mM with complete inhibition at 100 mM. Dermaseptin-L1 showed selective cytolytic activity against HepG2 human hepatoma-derived cells (LC 50 ¼ 45 mM) compared with human erythrocytes (LC 50 ¼ 200 mM) whereas phylloseptin-L1 was approximately equipotent against both HepG2 cells (LC 50 ¼ 35 mM) and erythrocytes (LC 50 ¼ 40 mM).
Post-secretory events alter the peptide content of the skin secretion of< i> Hypsiboas raniceps
2008
A novel family of antimicrobial peptides, named raniseptins, has been characterized from the skin secretion of the anuran Hypsiboas raniceps. Nine cDNA molecules have been successfully cloned, sequenced, and their respective polypeptides were characterized by mass spectrometry and Edman degradation. The encoded precursors share structural similarities with the dermaseptin prepropeptides from the Phyllomedusinae subfamily and the mature 28-29 residue long peptides undergo further proteolytic cleavage in the crude secretion yielding consistent fragments of 14-15 residues. The biological assays performed demonstrated that the Rsp-1 peptide has antimicrobial activity against different bacterial strains without significant lytic effect against human erythrocytes, whereas the peptide fragments generated by endoproteolysis show limited antibiotic potency. MALDI imaging mass spectrometry in situ studies have demonstrated that the mature raniseptin peptides are in fact secreted as intact molecules within a defined glandular domain of the dorsal skin, challenging the physiological role of the observed raniseptin fragments, identified only as part of the crude secretion. In this sense, stored and secreted antimicrobial peptides may confer distinct protective roles to the frog.
Peptides, 2010
Peptidomic analysis of norepinephrine-stimulated skin secretions of the South-East Asian frog Hylarana erythraea (formerly Rana erythraea partim) has led to the identification of multiple peptides with antimicrobial activity. Structural characterization of the peptides demonstrated that they belong to the brevinin-1 (3), brevinin-2 (2), esculentin-2 (4), and temporin (1) families. The values in parentheses indicate the number of paralogs. In addition, a peptide (GVIKSVLKGVAKTVALG ML.NH(2)) was isolated that shows some structural similarity to the brevinin-2-related peptides (B2RP) previously isolated from North American frogs of the genus Lithobates. A synthetic replicate of the species B2RP showed broad-spectrum growth inhibitory activity against reference strains of Escherichia coli (MIC=12.5 microM), Staphylococcus aureus (MIC=12.5 microM) and Candida albicans (MIC=50 microM) and was active against multidrug-resistant clinical isolates of Acetinobacter baumannii (MIC in the range...