Parasin I (TFA) is a 19-amino acid histone H2A-derived peptide isolated from the skin of the catfish, and shows antimicrobial activity.
CAT No: R1605
Parasin I TFA is a synthetic antimicrobial peptide derived from the skin mucus of the Japanese flounder (Paralichthys olivaceus), belonging to the class of cationic host defense peptides. Characterized by its amphipathic structure and net positive charge, Parasin I TFA exhibits potent membrane-disruptive properties against a broad spectrum of microorganisms. Its unique sequence and physicochemical attributes have made it an important subject in the study of innate immune responses and peptide-based antimicrobial strategies. The trifluoroacetate (TFA) salt form ensures enhanced solubility and stability, facilitating its use in a variety of biochemical and biophysical research contexts.
Antimicrobial mechanism studies: Parasin I TFA serves as a valuable tool in elucidating the molecular mechanisms of peptide-mediated microbial inhibition. Its ability to interact with and disrupt microbial membranes allows researchers to investigate the fundamental processes underlying membrane permeabilization, pore formation, and cell lysis. By employing this peptide in in vitro assays, scientists can dissect the sequence-activity relationships and structural determinants that govern the efficacy of cationic antimicrobial peptides, contributing to the broader understanding of host-pathogen interactions.
Peptide engineering and design: The sequence and structural features of Parasin I TFA provide a template for rational design and optimization of novel antimicrobial peptides. Researchers utilize it as a reference compound to guide synthetic modifications, such as amino acid substitutions or cyclization, aiming to enhance antimicrobial potency, selectivity, or proteolytic stability. Comparative studies involving Parasin I and its analogs enable the development of next-generation peptides with improved pharmacological profiles for research use in combating microbial resistance.
Innate immunity research: As a representative fish-derived defense peptide, Parasin I TFA is frequently employed in studies exploring the evolution and function of innate immune systems across vertebrates. Its activity profile and gene regulation patterns offer insights into the conserved mechanisms of first-line immune defense in aquatic organisms. Investigations using Parasin I contribute to the identification of immune effector pathways, modulation of inflammatory responses, and the discovery of new antimicrobial factors relevant to comparative immunology.
Biofilm inhibition assays: The peptide has demonstrated capacity to interfere with the formation and persistence of microbial biofilms, which are notoriously resistant to conventional antimicrobial agents. By incorporating Parasin I TFA into biofilm models, researchers can assess its efficacy in preventing initial bacterial adhesion, disrupting established biofilms, and reducing microbial viability within these complex communities. Such studies are essential for understanding peptide-based strategies to mitigate biofilm-associated problems in industrial, environmental, and biomedical settings.
Peptide structure-function analysis: Parasin I TFA is extensively used in biophysical and structural studies aimed at correlating peptide conformation with biological activity. Techniques such as circular dichroism spectroscopy, nuclear magnetic resonance, and fluorescence assays enable detailed examination of its secondary structure, membrane binding properties, and conformational dynamics in different environments. These analyses provide critical data for mapping functional domains, understanding peptide-lipid interactions, and informing the rational development of synthetic antimicrobial peptides with tailored properties for research applications.
4. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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