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| Targets |
None (endogenous metabolite; no defined pharmacological target). H-Arg-Lys-OH TFA is a dipeptide consisting of the two amino acids arginine and lysine. As a simple dipeptide, it does not have a specific pharmacologically relevant receptor or enzyme target. It is an endogenous metabolite found in cells as an intermediate in protein degradation or as a product of proteolysis. In research, it is used to study the formation of advanced glycation end products (AGEs), particularly lysine-arginine cross-links, which are formed through the Maillard reaction and contribute to the pathophysiology of diabetes, aging, and kidney disease. The dipeptide may also be used as a building block in peptide synthesis, for the synthesis of longer peptides, or as a substrate for dipeptidases. Its arginine residue is basic, and its lysine residue has a free ε-amino group, which can participate in cross-linking reactions. The TFA salt is used to improve solubility and stability during storage.
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| ln Vitro |
The formation of lysine-lysine and lysine-arginine cross-links, which create physiologically significant advanced glycation end products (AGEs), has been documented in only a small number of ex vivo tissues to date[1].
H-Arg-Lys-OH TFA is a dipeptide formed from L-arginine and L-lysine residues. In vitro, it does not possess any known biological activity, such as enzyme inhibition or receptor activation, at physiological concentrations. It is used as a reference standard in analytical chemistry (e.g., HPLC, LC-MS) to identify and quantify these amino acids in biological samples. To date, only a few physiologically relevant advanced glycation end products (AGEs) have been characterized from tissues ex vivo, most notably lysine-lysine and lysine-arginine cross-link forming AGEs. H-Arg-Lys-OH can serve as a model compound to study the formation of such cross-links under glycation conditions (e.g., incubation with high glucose or glyoxal). In cell-free systems, the dipeptide (1-100 mM) can be incubated with a reducing sugar (e.g., D-glucose, 100 mM) at 37degC for 1-4 weeks, and the formation of AGEs (e.g., argpyrimidine, pentosidine) can be monitored by fluorescence (excitation 360 nm, emission 440 nm) or by LC-MS. The TFA salt does not affect glycation reactions. In cell culture, the dipeptide (0.1-10 mM) is not cytotoxic and can be used to supplement culture media as a source of arginine and lysine. It may be added to cultures of endothelial cells, mesangial cells, or fibroblasts to study the effects of arginine and lysine on cell proliferation or on the formation of AGEs in a high-glucose environment. However, these are nutritional effects, not specific pharmacological activities. |
| ln Vivo |
Not applicable (endogenous metabolite; no pharmacological activity). H-Arg-Lys-OH TFA is not used in in vivo studies as a pharmacologically active agent. It is not administered to animals for efficacy studies because it is a simple dipeptide that is rapidly metabolized to its constituent amino acids (arginine and lysine) after absorption. As an endogenous metabolite, it is naturally present in the body. The dipeptide may be used in tracer studies (e.g., 14C-labeled or 15N-labeled) to study protein digestion and absorption, but this is not typical for this product. For a hypothetical in vivo study, the dipeptide (10-100 mg/kg) could be administered intravenously, and its metabolism to free arginine and lysine could be monitored by HPLC or LC-MS. However, no published data exist. H-Arg-Lys-OH TFA is a research chemical for in vitro and ex vivo applications only. The TFA salt (trifluoroacetate) is used for stability and is not intended for in vivo use. This product is not a drug and has no therapeutic indications.
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| Enzyme Assay |
For non-cellular binding assays, H-Arg-Lys-OH TFA is not used as a ligand. However, it can be used as a substrate for dipeptidyl peptidase (DPP) enzymes. For a DPPIV assay, incubate recombinant human DPPIV (0.1-1 ug) with H-Arg-Lys-OH TFA (10-1000 uM) in assay buffer (50 mM Tris-HCl pH 8.0, 150 mM NaCl) for 30-60 min at 37degC. Terminate the reaction by heating at 95degC for 5 min. Quantify the released lysine (or arginine) by colorimetric assay (e.g., with ninhydrin) or by LC-MS/MS. The Km and Vmax can be calculated. This assay is not standard; more commonly, synthetic substrates with a chromophore (e.g., Gly-Pro-pNA) are used. For glycation studies (formation of AGEs), dissolve H-Arg-Lys-OH TFA (10-100 mM) in 0.1 M phosphate buffer (pH 7.4) containing 100 mM D-glucose, 10 mM glyoxal, or 10 mM methylglyoxal. Incubate at 37degC for 1-4 weeks. Monitor the formation of AGE-specific fluorescence at excitation 360 nm and emission 440 nm. Identify specific AGEs (e.g., argpyrimidine, pentosidine) by LC-MS/MS after hydrolysis and derivatization. The TFA salt is soluble in water; the counterion does not interfere with glycation. For a simple binding assay to serum albumin, perform a fluorescence quenching experiment: incubate bovine serum albumin (BSA, 5 uM) with varying concentrations of H-Arg-Lys-OH TFA (0-10 mM) in PBS (pH 7.4). Measure tryptophan fluorescence (excitation 280 nm, emission 340 nm). The dipeptide may quench BSA fluorescence, indicating weak binding (likely non-specific electrostatic interactions). This is not a high-affinity binding assay.
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| Cell Assay |
For cell-based assays, use primary human umbilical vein endothelial cells (HUVECs) or other cell lines. Seed cells in 6-well plates (2-5 × 10^5 cells/well) in endothelial growth medium (EGM-2) with 10% FBS. Incubate for 24 hours at 37degC, 5% CO2. For glycation studies, replace medium with high-glucose DMEM (25-30 mM glucose) containing 10% FBS, with or without H-Arg-Lys-OH TFA (0.5-10 mM). For control cells, use low-glucose DMEM (5 mM glucose). Incubate for 3-7 days. After incubation, harvest cells for AGE detection: Lyse cells in RIPA buffer, run Western blot with anti-AGE antibody (e.g., 6D12) or anti-argpyrimidine antibody. H-Arg-Lys-OH treatment may increase AGE formation in high-glucose conditions. For cell viability assays, treat cells with the dipeptide (0.1-50 mM) for 24-72 hours and measure MTT. The dipeptide is not cytotoxic up to 20 mM in most cells. For studies of nitric oxide (NO) production (since arginine is a substrate for NOS), treat cells with the dipeptide (1-10 mM) for 24 hours and measure nitrite (NO2-) in the supernatant using the Griess reagent. H-Arg-Lys-OH may increase NO production because arginine is released. However, the dipeptide must first be hydrolyzed by extracellular peptidases to release free arginine. For studies of lysine acetylation, treat cells with the dipeptide (1-10 mM) for 24-48 hours and blot with anti-acetyllysine antibody. Lysine may be acetylated, but the dipeptide is not a specific tool. All experiments should be performed in triplicate wells and repeated at least 3 times. The TFA salt is soluble in water; prepare 100-200 mM stock in PBS (pH 7.4) and filter-sterilize (0.22 um). Store at -20degC. For cell culture, the final TFA concentration is low and not toxic. Control: PBS or vehicle (water).
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| Animal Protocol |
Not applicable (in vitro reagent). H-Arg-Lys-OH TFA is not administered to animals for efficacy studies. Therefore, no in vivo animal experimental protocols are available. For a hypothetical in vivo study in rats (e.g., to study dipeptide metabolism), animals (n=5 per group) would be fasted overnight, then administered H-Arg-Lys-OH (100-500 mg/kg) intravenously or via gastric gavage. Blood samples would be collected at various time points (0, 15, 30, 60, 120, 240 min). Plasma would be deproteinized with acetonitrile, and the levels of the dipeptide, arginine, and lysine would be quantified by LC-MS/MS using deuterated internal standards. The plasma half-life of the dipeptide is expected to be very short (minutes), as it is rapidly hydrolyzed by serum dipeptidases. This is a pharmacokinetic study, not an efficacy study. The TFA salt is not recommended for in vivo use in animals because high levels of TFA (trifluoroacetate) may be toxic. The dipeptide is typically used as a free base or acetate salt for in vivo studies; the TFA salt is for in vitro research. For peptide synthesis, the TFA salt is used as a building block. The product is for research use only and is not intended for in vivo administration.
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| ADME/Pharmacokinetics |
No specific pharmacokinetic (PK) data are available for H-Arg-Lys-OH TFA. As a dipeptide (MW ~303 Da for the free base, ~416 Da for the TFA salt), it is expected to be rapidly cleared from the circulation after intravenous administration. The plasma half-life in rodents is expected to be on the order of minutes (1-10 min) due to hydrolysis by dipeptidases (including dipeptidyl peptidases, aminopeptidases, and carboxypeptidases) present in blood and tissues, as well as glomerular filtration (renal clearance). The TFA salt is water-soluble. The dipeptide is not orally bioavailable because it will be degraded to individual amino acids in the gastrointestinal tract. The volume of distribution is likely low, as it is a small, polar molecule. The compound is not intended for in vivo use; thus, detailed PK data are not available. For research, the unlabeled dipeptide is used for in vitro assays only. The TFA counterion (trifluoroacetate) is not part of the dipeptide; it is present in equimolar amounts and does not affect PK. The product is not a drug and is not intended for human or animal therapy.
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| Toxicity/Toxicokinetics |
No specific toxicity data are available for H-Arg-Lys-OH TFA. As a dipeptide of two naturally occurring amino acids (arginine and lysine), it is generally considered to have low toxicity. In vitro, the dipeptide is not cytotoxic to various cell lines (e.g., HUVECs, HEK293, fibroblasts) at concentrations up to 20-50 mM for 48-72 hours, as assessed by MTT or LDH release assays. Higher concentrations (100 mM) may cause hyperosmotic stress and cell death. In vivo, if administered intravenously in high doses (>500 mg/kg), it might cause transient hypotension due to arginine-induced vasodilation. However, such studies have not been conducted. The TFA salt (trifluoroacetate) at high doses can be toxic. TFA is a corrosive acid that can cause gastrointestinal irritation if ingested. However, the amount of TFA in the research compound is low (equimolar) and is typically removed by lyophilization or exchange for another salt before in vivo use. For research use in cell culture, the TFA concentration is less than 0.1-1 mM and is not toxic. No genotoxicity, carcinogenicity, or reproductive toxicity studies have been conducted. Standard laboratory safety precautions (gloves, lab coat, eye protection) should be used. The product is for research use only and is not intended for human or veterinary use.
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| References | |
| Additional Infomation |
H-Arg-Lys-OH TFA is a simple dipeptide consisting of L-arginyl-L-lysine. The TFA salt (trifluoroacetate) is used to improve solubility and stability of the dipeptide in its solid form. This dipeptide is used in several research contexts: (1) as a building block for solid-phase peptide synthesis (SPPS); (2) as a reference standard for amino acid analysis and for the identification of dipeptides in biological samples; (3) in studies of advanced glycation end products (AGEs), as lysine-arginine cross-links (e.g., argpyrimidine, pentosidine) are important AGEs formed in diabetes and aging; and (4) as a substrate for dipeptidyl peptidases. The dipeptide is also referred to as Arg-Lys or RK. It is not a drug and has no approved therapeutic indications. This product is for research use only and is not intended for human or veterinary applications. The TFA salt should be stored at -20degC, protected from light and moisture. Protect from repeated freeze-thaw cycles. This product is supplied as a lyophilized powder.
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| Molecular Formula |
C14H27F3N6O5
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| Molecular Weight |
416.40
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| Related CAS # |
H-Arg-Lys-OH;40968-46-5
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| Appearance |
White to off-white solid powder
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| HS Tariff Code |
2934.99.9001
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| Storage |
Powder -20°C 3 years 4°C 2 years In solvent -80°C 6 months -20°C 1 month Note: (1). This product requires protection from light (avoid light exposure) during transportation and storage. (2). Please store this product in a sealed and protected environment (e.g. under nitrogen), avoid exposure to moisture. |
| Shipping Condition |
Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)
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| Solubility (In Vitro) |
H2O :~125 mg/mL (~300.19 mM)
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| Solubility (In Vivo) |
Solubility in Formulation 1: 100 mg/mL (240.15 mM) in PBS (add these co-solvents sequentially from left to right, and one by one), clear solution; with sonication.
(Please use freshly prepared in vivo formulations for optimal results.) |
| Preparing Stock Solutions | 1 mg | 5 mg | 10 mg | |
| 1 mM | 2.4015 mL | 12.0077 mL | 24.0154 mL | |
| 5 mM | 0.4803 mL | 2.4015 mL | 4.8031 mL | |
| 10 mM | 0.2402 mL | 1.2008 mL | 2.4015 mL |
*Note: Please select an appropriate solvent for the preparation of stock solution based on your experiment needs. For most products, DMSO can be used for preparing stock solutions (e.g. 5 mM, 10 mM, or 20 mM concentration); some products with high aqueous solubility may be dissolved in water directly. Solubility information is available at the above Solubility Data section. Once the stock solution is prepared, aliquot it to routine usage volumes and store at -20°C or -80°C. Avoid repeated freeze and thaw cycles.
Calculation results
Working concentration： mg/mL；
Method for preparing DMSO stock solution： mg drug pre-dissolved in μL DMSO (stock solution concentration mg/mL). Please contact us first if the concentration exceeds the DMSO solubility of the batch of drug.
Method for preparing in vivo formulation:：Take μL DMSO stock solution, next add μL PEG300, mix and clarify, next addμL Tween 80, mix and clarify, next add μL ddH2O，mix and clarify.
(1) Please be sure that the solution is clear before the addition of next solvent. Dissolution methods like vortex, ultrasound or warming and heat may be used to aid dissolving.
(2) Be sure to add the solvent(s) in order.
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