Octaarginine Trifluoroacetate

Octaarginine Trifluoroacetate contains eight sequential arginine residues, producing a highly cationic chain frequently investigated for transport and binding behavior. Strong guanidinium interactions enable studies of membrane translocation and nucleic acid association. The trifluoroacetate form improves handling and solubility. Research spans cargo-delivery models, peptide chemistry, and cell-penetration mechanism analysis.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Octaarginine Trifluoroacetate(CAS 148796-86-5)

CAT No: R2324

CAS No:148796-86-5

Synonyms/Alias:Octaarginine Trifluoroacetate;148796-86-5;Octa-arginine;

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M.F/Formula
C50H99F3N32O11
M.W/Mr.
1381.5
Sequence
One Letter Code:RRRRRRRR
Three Letter Code:H-Arg-Arg-Arg-DL-Arg-Arg-Arg-Arg-Arg-OH.TFA

Octaarginine Trifluoroacetate is a synthetic peptide comprised of eight consecutive arginine residues, typically presented as the trifluoroacetate salt to ensure stability and solubility. As a cell-penetrating peptide (CPP), it is renowned for its remarkable ability to traverse cellular membranes, enabling efficient intracellular delivery of various biomolecules. The guanidinium-rich structure of octaarginine confers strong electrostatic interactions with the negatively charged cell surface, which underpins its translocation capabilities. Owing to these properties, octaarginine has become a valuable tool in biochemical research, molecular biology, and drug discovery, where intracellular access is often a significant experimental bottleneck.

Intracellular delivery: Octaarginine serves as a highly effective carrier for the transport of diverse molecular cargoes, including peptides, proteins, nucleic acids, and small molecules, into live cells. Its cell-penetrating properties are particularly advantageous in studies requiring direct cytosolic or nuclear access, where traditional delivery methods often fall short due to membrane impermeability. By forming non-covalent or covalent complexes with target molecules, octaarginine facilitates their uptake via endocytosis and, in some cases, direct translocation, thereby expanding the scope of experimental design in cellular and molecular research.

Molecular imaging: The peptide's ability to ferry imaging probes and fluorescent markers across cellular membranes has made it indispensable in live-cell imaging and subcellular localization studies. When conjugated to fluorophores or contrast agents, octaarginine enables real-time visualization of intracellular processes, trafficking pathways, and biomolecular interactions without the need for invasive techniques. This application is particularly valuable for elucidating dynamic cellular events and validating delivery efficiency in various model systems.

Gene modulation studies: In the context of genetic research, octaarginine has been exploited for the delivery of oligonucleotides, siRNA, and antisense molecules into eukaryotic cells. Its efficient translocation properties help overcome the challenges posed by the negatively charged cell membrane, allowing for robust gene silencing or modulation experiments. By improving the intracellular availability of nucleic acid-based tools, octaarginine enables more precise manipulation of gene expression and functional genomics investigations.

Peptide functionalization: Octaarginine is routinely used as a functional tag to enhance the bioavailability and cellular uptake of otherwise impermeable peptides and proteins. Through chemical conjugation, it imparts cell-penetrating properties to therapeutic candidates, research probes, or engineered biomolecules, broadening their experimental utility. This strategy is especially relevant in the development of peptide-based research tools and in studies aiming to dissect intracellular signaling pathways or protein-protein interactions.

Biophysical studies: The unique interaction of octaarginine with lipid bilayers and cellular membranes also makes it a subject of interest in membrane biophysics and peptide-membrane interaction research. Investigations into its translocation mechanism, membrane binding affinity, and structural dynamics contribute to a deeper understanding of CPP function and inform the rational design of next-generation delivery vectors. Such studies are crucial for optimizing peptide-based delivery systems and advancing the field of targeted molecular transport.

InChI
InChI=1S/C48H98N32O9.C2HF3O2/c49-25(9-1-17-66-41(50)51)33(81)74-26(10-2-18-67-42(52)53)34(82)75-27(11-3-19-68-43(54)55)35(83)76-28(12-4-20-69-44(56)57)36(84)77-29(13-5-21-70-45(58)59)37(85)78-30(14-6-22-71-46(60)61)38(86)79-31(15-7-23-72-47(62)63)39(87)80-32(40(88)89)16-8-24-73-48(64)65;3-2(4,5)1(6)7/h25-32H,1-24,49H2,(H,74,81)(H,75,82)(H,76,83)(H,77,84)(H,78,85)(H,79,86)(H,80,87)(H,88,89)(H4,50,51,66)(H4,52,53,67)(H4,54,55,68)(H4,56,57,69)(H4,58,59,70)(H4,60,61,71)(H4,62,63,72)(H4,64,65,73);(H,6,7)/t25-,26-,27-,28?,29-,30-,31-,32-;/m0./s1
InChI Key
IZYRKBFCCCZTDD-GZNSWUDSSA-N

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