Temporin A features a short, hydrophobic peptide framework commonly associated with studies of membrane interaction and amphipathic folding. Its sequence promotes helical transitions in lipid-mimetic systems. Researchers analyze its solvent-dependent conformational states and binding equilibria. Applications span antimicrobial-peptide modeling, biophysical studies, and structural optimization.
CAT No: R2467
CAS No:188713-69-1
Synonyms/Alias:TEMPORIN A;188713-69-1;L-Phenylalanyl-L-leucyl-L-prolyl-L-leucyl-L-isoleucylglycyl-L-arginyl-L-valyl-L-leucyl-L-serylglycyl-L-isoleucyl-L-leucinamide;CHEMBL406865;Temporin A (FLPLIGRVLSGIL-amide);AKOS040757116;RS-2016;DA-78305;G14597;
Temporin A is a naturally occurring antimicrobial peptide originally isolated from the skin secretions of amphibians, particularly the European red frog Rana temporaria. As a member of the temporin family, it is characterized by a short amino acid sequence and a pronounced amphipathic alpha-helical structure, which underpins its membrane-active properties. Temporin A has garnered significant interest within the fields of peptide chemistry, microbiology, and membrane biophysics due to its ability to interact with and disrupt biological membranes. Its unique sequence and biophysical attributes make it a valuable tool for exploring host defense mechanisms, peptide-membrane interactions, and the development of novel antimicrobial strategies.
Antimicrobial mechanism studies: Temporin A is widely utilized in research focused on elucidating the molecular basis of antimicrobial action. Its ability to permeabilize and destabilize bacterial membranes provides a model system for investigating the structural and functional determinants of peptide-mediated microbial inhibition. By studying its interactions with lipid bilayers and bacterial cells, researchers can gain insight into the critical physicochemical parameters that govern selective toxicity and membrane perturbation, informing the rational design of next-generation antimicrobial peptides.
Peptide-membrane interaction assays: The distinctive amphipathic structure of temporin peptides makes Temporin A a preferred model for examining peptide-lipid interactions using biophysical techniques such as circular dichroism spectroscopy, fluorescence assays, and solid-state NMR. These studies contribute to a deeper understanding of how short, cationic peptides recognize, bind, and insert into biological membranes. Such insights are crucial for advancing peptide engineering efforts aimed at optimizing selectivity, potency, and stability for research and industrial applications.
Peptide structure-activity relationship (SAR) research: Temporin A serves as a foundational template for structure-activity relationship investigations, where systematic modifications to its amino acid sequence enable assessment of the impact on antimicrobial potency, cytotoxicity, and membrane affinity. By generating and testing analogs, researchers can delineate the contributions of specific residues to activity and selectivity, facilitating the development of tailored peptides with improved biochemical properties for use in basic research or as molecular tools.
Synthetic peptide development: The relatively simple sequence of Temporin A makes it an accessible candidate for solid-phase peptide synthesis, allowing for the production of both the native peptide and a wide array of derivatives. Its use in synthetic protocols provides valuable experience in optimizing peptide assembly, purification, and characterization workflows. Additionally, it functions as a benchmark compound for validating peptide synthesis methodologies and analytical techniques, supporting broader applications in peptide chemistry laboratories.
Antimicrobial resistance research: Temporin A is frequently employed in experimental models to study the interaction between host defense peptides and resistant microbial strains. By comparing its activity profile against sensitive and resistant bacteria, investigators can explore mechanisms of resistance emergence, peptide adaptation, and potential strategies to overcome reduced susceptibility. These studies are instrumental in informing the design of novel antimicrobial agents and in understanding the evolutionary pressures shaping microbial defense systems.
Through its diverse applications spanning antimicrobial mechanism elucidation, membrane biophysics, peptide engineering, synthetic methodology, and resistance research, Temporin A continues to be an indispensable resource for advancing peptide science and the broader field of host-pathogen interaction studies. Its well-characterized properties and versatility ensure ongoing relevance in both academic and industrial research environments.
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