Temporin A, amide

Product Name: Temporin A, amide

Sequence One Letter Code: FLPLIGRVLSGIL-NH2

Sequence Three Letter Code: H-Phe-Leu-Pro-Leu-Ile-Gly-Arg-Val-Leu-Ser-Gly-Ile-Leu-NH2

Chemical Formula:C68H117N17O14

Molecular Weight: 1396.9

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Bacterial

Source / Species: frog

Conjugation: Unconjugated

 Code Nacres: NA.26

Application: Temporin A, amide, is a short, highly hydrophobic antimicrobial peptide isolated from the frog Rana temporaria. It exhibits potent bactericidal activity against Gram-positive organisms, including antibiotic-resistant cocci. The peptide disrupts microbial membranes through amphipathic interactions that compromise membrane integrity and induce rapid cell death. In addition to its antimicrobial properties, Temporin A promotes chemotactic migration of human monocytes, macrophages, and neutrophils, linking direct pathogen killing with innate immune modulation. Synergistic effects have been observed when combined with other antimicrobial agents, enhancing its therapeutic relevance. Temporin A is widely used in studies of membrane–peptide interactions, host defense peptides, antimicrobial synergy, and the development of peptide-based strategies to combat resistant bacterial infections.

Current Research: The growing prevalence of antibiotic-resistant bacterial infections has intensified interest in antimicrobial peptides (AMPs) as potential alternatives or complements to conventional antibiotics. AMPs are naturally occurring components of innate immunity that provide rapid defense against pathogens through mechanisms distinct from traditional antimicrobial drugs. Among these peptides, Temporin A, originally isolated from the skin secretions of the frog Rana temporaria, has emerged as a widely studied example due to its potent antimicrobial activity and relatively simple structure. The C-terminally amidated form of Temporin A exhibits enhanced stability and biological activity, making it particularly useful in experimental investigations of antimicrobial mechanisms and host defense responses. A major focus of current research on Temporin A involves understanding its mechanism of membrane disruption. Temporin A is a short, highly hydrophobic peptide that adopts an amphipathic α-helical structure upon interacting with lipid membranes. This structural configuration enables the peptide to insert into bacterial membranes and destabilize lipid bilayers. Experimental studies using techniques such as fluorescence spectroscopy, circular dichroism, and solid-state NMR have shown that Temporin A interacts preferentially with membranes rich in negatively charged phospholipids, which are characteristic of bacterial cell envelopes. These interactions lead to membrane permeabilization, leakage of intracellular contents, and rapid bacterial cell death. Temporin A is particularly effective against Gram-positive bacteria, including clinically relevant pathogens such as Staphylococcus aureus and Enterococcus species. Importantly, several studies have demonstrated activity against antibiotic-resistant strains, including methicillin-resistant S. aureus (MRSA). Because its antimicrobial mechanism relies primarily on membrane disruption rather than specific metabolic targets, the likelihood of bacteria developing resistance through conventional mutation-based pathways is thought to be lower compared with many traditional antibiotics. Another significant area of research explores the immunomodulatory properties of Temporin A. In addition to directly killing microbes, the peptide can influence host immune responses by promoting chemotactic migration of immune cells, including human monocytes, macrophages, and neutrophils. These immune cells play crucial roles in pathogen clearance and inflammatory regulation. By attracting immune cells to sites of infection, Temporin A contributes to coordinated innate immune responses that combine direct antimicrobial activity with immune system activation. Current investigations also focus on synergistic interactions between Temporin A and other antimicrobial agents. When combined with conventional antibiotics or other host defense peptides, Temporin A can enhance antibacterial efficacy and reduce the concentrations of drugs required for microbial inhibition. Such synergistic effects have been reported in studies evaluating peptide–antibiotic combinations against resistant bacterial strains. These findings are particularly relevant for developing combination therapies aimed at overcoming antimicrobial resistance. Another active research area involves studying structure–activity relationships and peptide optimization. Because Temporin A is relatively short and structurally simple, it provides an attractive scaffold for designing modified peptides with improved stability, selectivity, or antimicrobial potency. Researchers frequently synthesize analogs with altered hydrophobicity, charge distribution, or sequence length to evaluate how these factors influence membrane interaction and antibacterial activity. These studies contribute to the broader effort to develop next-generation antimicrobial peptides suitable for therapeutic applications. Temporin A is also widely used as a model system for investigating membrane–peptide interactions. Its strong affinity for lipid bilayers makes it useful for studying how peptides interact with different membrane compositions, including bacterial versus mammalian membranes. Insights from these experiments help clarify the physicochemical principles that govern selective toxicity toward microbes while minimizing damage to host cells. In summary, Temporin A, amide remains an important peptide in antimicrobial research. Its potent activity against Gram-positive bacteria, ability to disrupt microbial membranes, and capacity to modulate immune responses make it a valuable model for studying host defense peptides. Through applications in membrane biophysics, antimicrobial synergy studies, and peptide engineering, Temporin A continues to contribute to the development of innovative strategies aimed at addressing the global challenge of antibiotic resistance.