Dermaseptin, a peptide isolated from frog skin, exhibits potent antimicrobial activity against bacteria, fungi and protozoa.
CAT No: R1323
CAS No:136212-91-4
Synonyms/Alias:Dermaseptin;136033-70-0;Dermaseptin S;136212-91-4;Dermaseptin I;dermaseptin S1;Dermaseptin DS 01;MFCD00146655;Dermaseptin from Phyllomedusa sauvagii;Dermaseptin S3(1-16);Dermaseptin S trifluoroacetate;Dermaseptin 1 trifluoroacetate;CHEMBL525200;FD73351;DA-62782;Dermaseptin (H-L-Ala-L-Leu-L-Trp-L-Lys-L-Thr-L-Met-L-Leu-L-Lys-L-Lys-L-Leu-Gly-L-Thr-L-Met-L-Ala-L-Leu-L-His-L-Ala-Gly-L-Lys-L-Ala-L-Ala-L-Leu-Gly-L-Ala-L-Ala-L-Ala-L-Asp-L-Thr-L-Ile-L-Ser-L-Gln-Gly-L-Thr-L-Gln-OH);L-Glutamine, L-alanyl-L-leucyl-L-tryptophyl-L-lysyl-L-threonyl-L-methionyl-L-leucyl-L-lysyl-L-lysyl-L-leucylglycyl-L-threonyl-L-methionyl-L-alanyl-L-leucyl-L-histidyl-L-alanylglycyl-L-lysyl-L-alanyl-L-alanyl-L-leucylglycyl-L-alanyl-L-alanyl-L-alanyl-L-.alpha.-aspartyl-L-threonyl-L-isoleucyl-L-seryl-L-glutaminylglycyl-L-threonyl-;NH2-Ala-Leu-Trp-Lys-Thr-Met-Leu-Lys-Lys-Leu-Gly-Thr-Met-Ala-Leu-His-Ala-Gly-Lys-Ala-Ala-Leu-Gly-Ala-Ala-Ala-Asp-Thr-Ile-Ser-Gln-Gly-Thr-Gln-COOH;
Dermaseptin is a naturally occurring antimicrobial peptide originally isolated from the skin secretions of certain frog species, most notably Phyllomedusa sauvagii. As a member of the host-defense peptide family, it is characterized by its amphipathic α-helical structure and broad-spectrum bioactivity against bacteria, fungi, protozoa, and some enveloped viruses. Its unique sequence and membrane-disruptive mechanism have captured the interest of researchers exploring innate immunity, peptide-membrane interactions, and the development of bioactive agents. The peptide's robust lytic activity, stability in biological environments, and adaptability to sequence modifications make it a valuable tool in a variety of biochemical and biotechnological investigations.
Antimicrobial research: Dermaseptin is widely utilized in studies of antimicrobial mechanisms and peptide-based defense strategies. Its rapid bactericidal action via membrane permeabilization provides a model system for dissecting how host-defense peptides disrupt microbial membranes. Researchers employ it to evaluate the efficacy of novel peptide analogs, investigate resistance mechanisms in pathogenic microbes, and characterize the structure-activity relationships that govern selective toxicity. Its broad-spectrum activity also makes it a reference compound in comparative analyses of antimicrobial peptides from diverse origins.
Peptide-membrane interaction studies: The peptide's amphipathic nature and ability to form α-helical structures upon membrane contact make it an ideal probe for examining peptide-lipid interactions. Biophysical and biochemical assays employing dermaseptin yield insights into peptide insertion, aggregation, and pore formation within phospholipid bilayers. Such studies underpin the development of membrane-active agents and inform the rational design of peptides with tailored selectivity and potency. Additionally, its well-characterized biophysical properties support investigations into factors influencing peptide-induced membrane destabilization.
Peptide engineering and synthetic biology: Due to its modular sequence and amenability to modification, dermaseptin serves as a template for the rational design of novel peptides with enhanced activity, stability, or specificity. Researchers leverage its structure to generate libraries of analogs for screening against multidrug-resistant pathogens or to optimize physicochemical properties for specific applications. In synthetic biology, it is incorporated into chimeric constructs or fusion proteins to impart antimicrobial or membrane-disruptive functions to engineered biomolecules.
Biofilm inhibition assays: The peptide's ability to disrupt microbial communities extends to the inhibition and eradication of biofilms, which are notoriously resistant to conventional antimicrobial agents. In vitro biofilm models utilize dermaseptin to assess its capacity to prevent biofilm formation or to disperse established biofilms on abiotic surfaces. These studies are critical for understanding the molecular determinants of biofilm resistance and for developing strategies to combat persistent microbial colonization in industrial and research settings.
Analytical standard in peptide research: Dermaseptin is frequently employed as a reference standard in peptide analytics, including high-performance liquid chromatography (HPLC), mass spectrometry, and circular dichroism spectroscopy. Its defined sequence and reproducible physicochemical properties facilitate method development, instrument calibration, and quality control in peptide synthesis and purification workflows. By serving as a benchmark, it enhances the reliability and comparability of analytical results across laboratories engaged in peptide science.
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