RNAIII-inhibiting peptide(TFA)

RNAIII-inhibiting peptide(TFA) is a potent inhibitor of Staphylococcus aureus, effective in the diseases such as cellulitis, keratitis, septic arthritis, osteomylitis and mastitis.

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

CAT No: R1661

Synonyms/Alias:RNAIII-inhibiting peptide(TFA);RNAIII-inhibiting peptide TFA;2703745-76-8;(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxypropanoyl]pyrrolidine-2-carbonyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-3-hydroxybutanoyl]amino]-N-[(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]butanediamide;2,2,2-trifluoroacetic acid;RNAIII-inhibiting peptide;HY-P1452A;RNAIII-INHIBITING PEPTIDETFA;EX-A8194;AKOS040763999;MS-31876;CS-0043429;G16493;

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cGMP Peptide
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M.F/Formula
C47H57F3N10O13
M.W/Mr.
1027
Sequence
One Letter Code:YSPWTNF
Three Letter Code:H-Tyr-Ser-Pro-Trp-Thr-Asn-Phe-NH2.TFA

RNAIII-inhibiting peptide (TFA) is a synthetic peptide compound designed to modulate quorum sensing mechanisms in Gram-positive bacteria, particularly Staphylococcus aureus. As a potent inhibitor of the RNAIII-activating pathway, it disrupts the agr (accessory gene regulator) system, which plays a critical role in the regulation of virulence factor expression and biofilm development. The trifluoroacetate (TFA) salt form enhances its solubility and stability, making it well-suited for precise experimental applications in molecular microbiology and bacterial pathogenesis research. By specifically targeting regulatory RNA signaling, this peptide offers a valuable tool for dissecting bacterial communication networks and exploring innovative strategies to control microbial behavior.

Quorum sensing research: RNAIII-inhibiting peptide is widely employed in studies investigating bacterial quorum sensing, the cell-to-cell communication process that regulates gene expression in response to population density. By competitively interfering with the agr system, the peptide enables researchers to modulate and analyze the downstream effects of disrupted signaling pathways. This facilitates the elucidation of molecular mechanisms underlying virulence regulation, population dynamics, and community interactions in Staphylococcus aureus and related species.

Biofilm formation studies: The peptide's ability to inhibit RNAIII activation makes it an effective reagent for exploring the relationship between quorum sensing and biofilm development. In vitro experiments utilizing this inhibitor allow scientists to examine how suppression of the agr system impacts biofilm architecture, maturation, and dispersal. Such studies are essential for understanding persistent bacterial colonization and for identifying new targets to mitigate biofilm-associated challenges in industrial, environmental, and biomedical contexts.

Virulence factor expression analysis: By blocking the activation of key regulatory RNAs, RNAIII-inhibiting peptide provides a precise means to study the expression of toxins, enzymes, and other virulence determinants. Researchers can employ the peptide in genetic, proteomic, or transcriptomic assays to quantify changes in virulence factor production under controlled conditions. This approach is instrumental in mapping regulatory networks and assessing the contribution of specific signaling pathways to pathogenic phenotypes.

Antimicrobial resistance research: Disruption of quorum sensing pathways with this peptide offers a unique perspective in the study of antimicrobial resistance mechanisms. By modulating the agr system, investigators can evaluate how altered cell signaling influences susceptibility to conventional antibiotics, adaptive responses, and the emergence of resistant subpopulations. These insights contribute to the development of novel anti-infective strategies that target bacterial communication rather than growth or viability.

Peptide-based inhibitor development: RNAIII-inhibiting peptide serves as a model compound for the design and optimization of next-generation peptide inhibitors targeting bacterial regulatory systems. Its well-characterized mode of action and specificity provide a foundation for structure-activity relationship studies, high-throughput screening, and rational engineering of analogs with improved potency or spectrum of activity. Such research supports the broader effort to develop innovative molecular tools and chemical probes for bacterial signaling research and biotechnological applications.

InChI
InChI=1S/C45H56N10O11.C2HF3O2/c1-24(57)38(44(65)52-34(21-37(47)59)41(62)50-32(39(48)60)19-25-8-3-2-4-9-25)54-42(63)33(20-27-22-49-31-11-6-5-10-29(27)31)51-43(64)36-12-7-17-55(36)45(66)35(23-56)53-40(61)30(46)18-26-13-15-28(58)16-14-26;3-2(4,5)1(6)7/h2-6,8-11,13-16,22,24,30,32-36,38,49,56-58H,7,12,17-21,23,46H2,1H3,(H2,47,59)(H2,48,60)(H,50,62)(H,51,64)(H,52,65)(H,53,61)(H,54,63);(H,6,7)/t24-,30+,32+,33+,34+,35+,36+,38+;/m1./s1
InChI Key
UFMWBLWECSYAKK-TUPMYQNZSA-N

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