Dermaseptin | CAS 136212-91-4 | Cationic Antimicrobial Peptide (Research Use Only) | Knowlux

Product Description

Dermaseptin, CAS 136212-91-4, is a synthetic 34-amino-acid cationic antimicrobial peptide corresponding to the naturally occurring host-defense peptide isolated from the skin of the South American frog Phyllomedusa sauvagii, supplied by Knowlux for laboratory research use. The peptide is linear, contains no cysteine or disulfide bonds, and carries a free C-terminal glutamine carboxylate. The molecular formula is C152H257N43O44S2 and the molecular weight is approximately 3455.1 g/mol on a free-peptide basis. Each lot is released with a lot-specific COA, MSDS and analytical traceability.

CAS and Salt Form Clarification: CAS 136212-91-4 is the free peptide registry for Dermaseptin and is the identifier applied across MedChemExpress, Creative Biolabs, ChemicalBook, TargetMol, Adooq, LKT Labs, and GenScript. A separate trifluoroacetate (TFA) salt registry circulates under CAS 646451-06-1 and should not be conflated with the free peptide. The molecular formula and weight are consistent across the principal sources at C152H257N43O44S2 and 3455.04 to 3455.10 g/mol, with two supplier discrepancies noted and corrected: one listing shows the formula as C125H25N43O42S2, which is a typographical corruption, and another shows the nitrogen count as N40 rather than N43, which is a formula-field error. The consensus C152H257N43O44S2 / 3455.1 assignment is adopted throughout this specification. Knowlux declares the salt form, counter-ion identity, and peptide content per lot on the COA. Buyers should confirm whether the quoted material is free peptide or TFA salt before procurement.

Structural and Mechanistic Note: Dermaseptin is a prototypical member of the membrane-damaging cationic peptide class. It undergoes a coil-to-helix transition upon binding to lipid bilayers, and its amphipathic alpha-helical structure enables interaction with and permeabilization of target cell membranes. The peptide is water-soluble, thermostable, and non-hemolytic at active concentrations, properties that distinguish it from many other membrane-active antimicrobial peptides. Dermaseptin contains Trp5, which provides a native UV chromophore at 280 nm; it contains no phenylalanine, no cysteine, and no disulfide. The two methionine residues (Met6 and Met13) are the principal oxidation liabilities. The absence of cysteine and disulfide bonds removes disulfide scrambling as a degradation pathway, and reducing agents are not required during handling.

Product Parameters

Product Details

1. Overview

Dermaseptin is a 34-residue host-defense peptide originally isolated from the skin of the frog Phyllomedusa sauvagii. It is the prototypical member of the dermaseptin family of cationic antimicrobial peptides and is characterized by broad-spectrum activity against pathogenic filamentous fungi, bacteria, yeasts, and protozoa. The peptide is cidal at micromolar concentrations and is described as water-soluble, thermostable, and non-hemolytic at active concentrations. Dermaseptin is used as a research tool in antimicrobial peptide pharmacology, membrane biophysics, and innate immunity. The material supplied under this specification is research-grade and is not intended for human administration.

2. Antimicrobial Mechanism and Spectrum

Dermaseptin exerts its antimicrobial action through a membrane-damaging mechanism rather than a specific receptor or enzyme target. As a cationic amphipathic peptide, it binds to negatively charged phospholipid bilayers, undergoes a conformational transition from random coil to alpha-helix, and permeabilizes the membrane, leading to loss of barrier function and cell death. The peptide is active against a wide spectrum of microorganisms at micromolar doses. Dermaseptins in the stricto sensu group are described as prototypical membrane-damaging cationic peptides with cidal activity against bacteria, fungi, yeasts, and protozoa. Subfamily-specific differences exist: dermaseptins S are active primarily against bacteria and form aggregates at high peptide-to-lipid ratios, whereas dermaseptins B are also active against fungi and form aggregates at low peptide-to-lipid ratios. Beyond direct antimicrobial action, Dermaseptin (DRs S1) stimulates the microbicidal activities of polymorphonuclear leukocytes (PMNs), including the respiratory burst and exocytosis, indicating an immunomodulatory component to its host-defense function. These descriptions are derived from published research and are provided for scientific reference only.

3. Research Applications

Published pharmacological characterizations and documented protocols describe the following research applications:

• Antimicrobial susceptibility testing against Gram-positive and Gram-negative bacteria, fungi, yeasts, and protozoa

• Membrane permeabilization and lipid bilayer interaction studies (coil-to-helix transition, membrane curvature strain)

• Structure-activity relationship studies of amphipathic alpha-helical antimicrobial peptides

• Innate immunity and polymorphonuclear leukocyte (PMN) activation research (respiratory burst, exocytosis)

• Biofilm inhibition and resistance profiling of membrane-active antimicrobial peptides

• Reference standard development for HPLC and LC-MS analytical methods

These descriptions are derived from published research and are provided for scientific reference only.

Quality Control

Solubility and Handling

Solubility: Dermaseptin solubility is documented in both water and DMSO, with the water value being the more extensively characterized condition. AbMole reports water solubility of 25 mg/mL at 25C with ultrasonic assistance. GLPBIO and ChemicalBook describe the peptide as soluble in DMSO, and ChemicalBook additionally lists a lyophilized powder form. For practical stock preparation, water at 25 mg/mL with sonication is the most consistently supported aqueous condition, and DMSO is a viable alternative where an organic vehicle is required. Prepare solutions fresh and aliquot to avoid repeated freeze-thaw cycles; MedChemExpress specifies that stock solutions are stable for 6 months at -80C or 1 month at -20C under sealed, moisture-free conditions.

Handling Precautions: Use powder-handling containment (glove box or fume hood with particulate control). Avoid inhalation of fine powder. Wear nitrile gloves, lab coat, and eye protection. The two methionine residues (Met6 and Met13) are susceptible to oxidation; handle under inert atmosphere where practical and avoid prolonged exposure to air and light. Reducing agents are not required because the peptide contains no cysteine or disulfide bonds.

Storage and Stability

Documentation Support

Per lot: COA, MSDS, HPLC chromatogram, and mass spectrometry data. Salt-form identity, counter-ion content, and peptide content available on request. Custom specifications and third-party inspection can be arranged on a project basis.

About Knowlux

Knowlux Biotechnology is a GMP-oriented manufacturer and supplier of peptides, APIs and fine-chemical research compounds, operating from Hubei, China. We serve research groups, CDMOs and distributors in more than 40 countries, and support contract synthesis, custom packaging and technical documentation requests.

Compliance Statement

FOR RESEARCH USE ONLY. NOT FOR HUMAN USE. NOT FOR DIAGNOSTIC OR THERAPEUTIC USE.

This product is supplied for laboratory research use only. It is not for human or animal administration, not for diagnostic or therapeutic use, not for retail sale, and not for personal use. Dermaseptin is not approved as a medicinal product in any jurisdiction. The purchaser is responsible for verifying product specifications against their specific research requirements and for compliance with all applicable institutional, local, and national regulations governing research chemical acquisition, storage, and use. Research context statements are for scientific reference only and do not constitute medical advice, promotional claims, or dosing guidance.

Data Verification Notes

The molecular formula C152H257N43O44S2 and molecular weight 3455.04 to 3455.10 are confirmed across Creative Biolabs, ChemicalBook, NovoPro, Adooq, LKT Labs, TargetMol, and GenScript. The sequence 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 is confirmed by Creative Biolabs, ChemicalBook, and TargetMol. The GLPBIO formula C125H25N43O42S2 is noted as a typographical corruption and not adopted. The MedChemExpress nitrogen count N40 rather than N43 is noted as a formula-field error and not adopted. The TFA salt CAS 646451-06-1 is from InvivoChem. The membrane-damaging coil-to-helix mechanism and the dermaseptin S versus B subfamily distinction are from the ScienceDirect and Europe PMC sources. The PMN respiratory burst and exocytosis data are from the ScienceDirect abstract. Solubility values are reported with their source and conditions. Storage shelf-life divergence (1 year versus 2 years at -20C for powder) is reported as-is; the -20C powder condition is the most widely supported archival temperature, and -80C is presented as the conservative option.

Formatting Note: All formulas, sequences, and comparison operators use plain ASCII notation to prevent character corruption on the platform. Section headings, table alignment, and spacing follow the approved product detail pattern. No trailing spaces or non-breaking characters are used; tables use consistent pipe alignment. No web links or hyperlinks are included in this document.