Tiger17

Tiger17 is an amphibian-derived peptide analogue containing cationic and hydrophobic residues that support membrane interaction. The sequence promotes α-helical formation under physiological conditions. Researchers explore its folding behavior and antimicrobial-like properties. Applications include host-defense peptide modeling, membrane disruption studies, and biophysical motif characterization.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R2817

Synonyms/Alias:HY-P10363;CS-1051506

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M.F/Formula
C62H99N21O11S2
M.W/Mr.
1378.7
Sequence
One Letter Code:WCKPKPKPRCH
Three Letter Code:H-Trp-Cys-Lys-Pro-Lys-Pro-Lys-Pro-Arg-Cys-His-NH2

Tiger17, a synthetic cationic peptide originally derived from amphibian skin secretions, has attracted significant attention in biochemical and pharmaceutical research due to its unique structural properties and broad-spectrum biological activity. Characterized by its amphipathic alpha-helical conformation, Tiger17 demonstrates remarkable stability and solubility under a variety of experimental conditions, making it an excellent candidate for diverse laboratory applications. Its sequence composition endows it with the ability to interact selectively with microbial membranes, distinguishing it from other antimicrobial peptides and enabling targeted studies on membrane dynamics and peptide-membrane interactions. Researchers value Tiger17 for its reproducible activity profiles and its versatility as a tool in both fundamental and applied sciences, where its mechanism of action and molecular interactions can be precisely elucidated through a range of experimental models.

Antimicrobial mechanism studies: Tiger17 serves as a powerful model peptide for investigating the mechanisms underlying antimicrobial activity at the molecular level. By incorporating it into in vitro assays, researchers can analyze how cationic peptides disrupt bacterial cell membranes, induce pore formation, and ultimately lead to cell lysis. The peptide's ability to preferentially bind to negatively charged microbial membranes over mammalian cell membranes provides valuable insights into the design of next-generation antimicrobial agents. Such studies not only advance the understanding of innate immune defense strategies but also inform the rational engineering of peptide analogs with enhanced specificity and reduced cytotoxicity.

Biofilm inhibition research: The peptide's efficacy in disrupting established biofilms and preventing their formation is of particular interest in the context of persistent bacterial infections and industrial biofouling. Scientists employ Tiger17 in microtiter plate biofilm assays, confocal microscopy, and flow cell systems to observe its effects on biofilm architecture and viability. By elucidating its mode of action—whether through direct disruption of the extracellular polymeric substance matrix or interference with quorum sensing pathways—researchers can identify potential strategies for combating biofilm-associated resistance, a major challenge in both clinical and environmental settings.

Peptide-membrane interaction modeling: Owing to its well-characterized sequence and amphipathic nature, Tiger17 is commonly used in computational and biophysical studies aimed at modeling peptide-lipid interactions. Techniques such as circular dichroism spectroscopy, nuclear magnetic resonance, and molecular dynamics simulations enable detailed analysis of how the peptide adopts helical conformations and inserts into lipid bilayers. These investigations contribute to a deeper understanding of the structure-activity relationships governing peptide function and facilitate the rational design of novel peptides with tailored membrane-targeting properties for use in drug delivery or antimicrobial applications.

Antimicrobial resistance research: The escalating problem of antibiotic resistance has prompted the exploration of alternative antimicrobial strategies, and Tiger17 stands out as a valuable research tool in this context. By subjecting various bacterial strains to repeated exposure to the peptide, scientists can monitor the development of resistance mechanisms and identify genetic or phenotypic adaptations that confer tolerance. Such studies provide critical data for assessing the long-term efficacy of peptide-based antimicrobials and guide the development of combination therapies or peptide modifications aimed at minimizing resistance emergence.

Immunomodulatory activity exploration: Beyond its direct antimicrobial effects, Tiger17 has been investigated for its potential to modulate immune responses in vitro. Researchers utilize cell culture assays to examine how the peptide influences cytokine production, chemotaxis, and immune cell activation, shedding light on its role in innate immunity. These findings open avenues for the development of multifunctional peptides that not only target pathogens but also enhance host defense mechanisms, offering new perspectives in immunological research and therapeutic innovation.

In summary, Tiger17 represents a multifaceted research tool with applications spanning antimicrobial mechanism elucidation, biofilm inhibition, peptide-membrane interaction modeling, antimicrobial resistance studies, and immunomodulatory activity exploration. Its unique structural and functional attributes make it indispensable for advancing our understanding of peptide biology and for informing the design of novel bioactive molecules. As research continues to uncover new facets of its activity, this synthetic peptide is poised to remain at the forefront of peptide-based scientific innovation, supporting efforts to address pressing challenges in microbiology, immunology, and biophysics.

InChI
InChI=1S/C62H99N21O11S2/c63-22-6-3-15-42(75-54(87)46(33-95)79-52(85)39(66)29-36-31-72-40-14-2-1-13-38(36)40)59(92)82-27-11-20-49(82)57(90)77-44(17-5-8-24-65)61(94)83-28-12-21-50(83)58(91)76-43(16-4-7-23-64)60(93)81-26-10-19-48(81)56(89)74-41(18-9-25-71-62(68)69)53(86)80-47(34-96)55(88)78-45(51(67)84)30-37-32-70-35-73-37/h1-2,13-14,31-32,35,39,41-50,72,95-96H,3-12,15-30,33-34,63-66H2,(H2,67,84)(H,70,73)(H,74,89)(H,75,87)(H,76,91)(H,77,90)(H,78,88)(H,79,85)(H,80,86)(H4,68,69,71)/t39-,41-,42-,43-,44-,45-,46-,47-,48-,49-,50-/m0/s1
InChI Key
DWALZAYVRAWAFV-QNPIOFFVSA-N

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