Medicines & Treatments
2mg Blue Xanax Bars
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Thymagen (20mg)
Thymagen, also known as EW (Glu-Trp), is a synthetically formulated bioregulator peptide, classified within the group of Khavinson peptides. It is an artificial peptide analog of the thymus-derived polypeptide, thymalin, and is noted for its potential immunomodulating characteristics. Thymagen’s role in immune system modulation is becoming increasingly recognized. It seems to interact with key immune processes, potentially modifying immune responses and defense mechanisms. This includes the possibility of altering immune cell activities and influencing the production of various cytokines. In cellular studies, Thymagen research has suggested its potential action on immune regulation, positing its involvement in reinforcing the natural defense mechanisms. Chemical Makeup Molecular formula: C16H19N3O5 Molecular weight: 333.3 g/mol Sequence: Glu-Trp Other known titles:Oglufanide, Thymogen Research and Clinical Studies Thymagen and Immune Cells The research on Thymagen may indicate a potential influence on cyclic nucleotide systems in murine models, which is particularly noted in the context of anaphylaxis and sensitization. In such models, Thymagen, along with other peptide substances with similar potential like thymalin and vilosen, possibly affects the catabolic processes of cyclic nucleotides. In sensitized animals, researchers have noted an apparent decrease in the ratio of cyclic adenosine monophosphate (cAMP) to cyclic guanosine monophosphate (cGMP). Thymagen's potential role in this process appears to be connected to a modulation of this ratio. When anaphylaxis occurs, the cAMP/cGMP ratio apparently returns to a reference level, implying a balancing action. Further, Thymagen may potentially contribute to the increased activity of enzymes responsible for cyclic nucleotide catabolism in lymphocytes of sensitized murine models. This tendency towards an increase is also posited in lymphocytes of murine models of anaphylaxis.(1) Apart from anaphylaxis and hypersensitivity models, Thymagen has also been researched regarding its potential action in models of bacterial infections. According to one trial, Thymagen may have a potential immunoregulatory action in murine models of Yersinia enterocolitica infection. This potential might include a reduction in the polyclonal immune response and the development of autoimmune reactions. Notably, Thymagen appeared to have promoted the intensive development of delayed hypersensitivity in a model of enteral infection with Yersinia enterocolitica. However, it is important to note that this action did not appear to manifest in all cases. Furthermore, Thymagen appeared to have enhanced the nonspecific resistance of the murine models. This enhancement may have potentially contributed to a decrease in the spread of the infective agents across various organs and tissues and facilitated their subsequent elimination from the murine models.(2) Thymagen may also have potential to regulate immunological processes, particularly in the context of T-lymphocyte differentiation and secondary immunodeficiency in experimental models of autoimmune conditions. It is posited that Thymogen may act to modulate certain immune responses, thereby reducing potential secondary immune deficit in these models. The researchers commented that “clinical effect […] was registered in 94.4%, laboratory effect in 83.3%” in tested models.(3) Other experiments have also investigated scenarios involving secondary immunodeficiency, particularly in models of fungal infections like candidiasis. The underlying hypothesis of one such study posits that Thymogen might possibly activate the immunocompetent system, including the thymus. This activation is thought to potentially contribute to the mitigation of the severity of candidiasis. In murine models, where secondary immunodeficiency is induced and followed by the development of candidiasis, Thymogen has been suggested to affect the course of the infection. The observations suggest that after exposure to Thymogen, the severity of candidiasis in these models might be reduced. This outcome implies that Thymogen may have a role in bolstering the immune response, particularly in fungal infection models.(4) Thymagen and Cardiac Cells Thymagen may have shown potential in addressing various types of arrhythmias in murine models. This potential has been posited through its examination in six distinct arrhythmia models. These models include those apparently induced by agents like aconitine, calcium chloride, strophanthin, scenarios of low sodium levels, reperfusion, and epinephrine administration. These agents are also known to induce ischaemia and therefore used to model arrhythmia. Yet, more trials are needed to evaluate and access these findings. The scientists specifically noted that “The mechanism of the Thymogen anti-ischemic action is realized without the participation of the opiate receptors and blockade of calcium entrance into the cardiomyocytes.”(5) Thymagen and Tumor Cells A study in murine models which underwent exposure of N-nitrososarcosine ethyl ester (NSEE) reported an apparent induction of the formation of papilloma cells and carcinoma cells in cultures from esophagus cell lines. The researchers reported that Thymagen apparently decreased the occurrence of such tumor cells by roughly 12% and seemingly reduced the tumor multiplicity by 1.7 times.(6) In another study involving murine models and Thymagen, the models were exposed to high levels of radiation exposure from radionuclide over 12 months, ultimately inducing the formation of cancer cells. Some of these models were also apparently introduced with Thymagen for five consecutive days each month, alongside the radionuclide exposure. The results from this study suggested that the murine models exposed to radionuclides alone exhibited a higher occurrence of tumor cells generally, and especially in cell lines from breast tissue. Conversely, in the rats that were also exposed to Thymagen alongside the radionuclides, there appeared to be a reduction in both the total number of tumor cells and their incidence. Furthermore, the study posited that murine models exposed only to Thymagen (without radionuclide exposure) appeared to exhibit an apparently longer lifespan, a slower aging rate, and a lower overall occurrence of tumor cells, both malignant and benignant. This finding may highlight Thymagen's potentially broader role in influencing aging and tumor development, beyond its apparent interaction with radiation-induced carcinogenesis.(7) A third study explored the potential of Thymagen, particularly focusing on its action on cellular immunity in the context of subjects with solid tumors in the abdominal cavity and retroperitoneal space, specifically before manual excision. Study findings following Thymagen exposure for seven days suggest that it may potentially aid in restoring the structural and functional parameters of cellular immunity, when compared to a placebo group. This potential is indicated by a reduction in the number and severity of complications observed in the study, as well as a possible shortening of the recovery period following an excision.(8) Thymagen peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Demidov, S. V., Kostromin, A. N., Kuĭbeda, V. V., Chernaia, I. V., & Borovok, M. I. (1991). Vliianie timagena, timalina i vilozena na soderzhanie cAMP, cGMP i aktivnost' fosfodiésteraz v limfotsitakh selezenki pri sensibilizatsii i anafilakticheskom shoke [Effect of thymagen, thymalin and vilosen on the cAMP and cGMP levels and phosphodiesterase activity in spleen lymphocytes during sensitization and anaphylactic shock]. Ukrainskii biokhimicheskii zhurnal (1978), 63(4), 104–106. https://pubmed.ncbi.nlm.nih.gov/1659006/ Iushchuk, N. D., Tseneva, G. I.a, Alenushkina, T. V., & Kuliashova, L. B. (1995). Effektivnost' primeneniia timogena pri éksperimental'noĭ infektsii, vyzvannoĭ Yersinia enterocolitica [The efficacy of using thymogen in an experimental infection caused by Yersinia enterocolitica]. Zhurnal mikrobiologii, epidemiologii i immunobiologii, (3), 106–108. https://pubmed.ncbi.nlm.nih.gov/7660690/ Zhuk, E. A., & Galenok, V. A. (1996). Timogen v lechenii sakharnogo diabeta I tipa [Thymogen in the treatment of type-1 diabetes mellitus]. Terapevticheskii arkhiv, 68(10), 12–14. https://pubmed.ncbi.nlm.nih.gov/9026934/ Khmel'nitskiĭ, O. K., Iakovlev, G. M., Belianin, V. L., Khavinson, V. K.h, Morozov, V. G., & Deĭgin, V. I. (1990). Vliianie sinteticheskogo peptida timusa (timogena) na immunnuiu sistemu pri kandidoze v usloviiakh immunodepressii [The effect of a synthetic thymus peptide (thymogen) on the immune system in candidiasis under immunodepression]. Arkhiv patologii, 52(1), 20–25. https://pubmed.ncbi.nlm.nih.gov/2337388/ Filippova, O. V., Reznikov, K. M., Alabovskił, V. V., Khamburov, V. V., & Vinokurov, A. A. (1997). Vliianie timogena na sostoianie serdtsa pri ishemii i reperfuzii [The effect of thymogen on the heart in ischemia and reperfusion]. Eksperimental'naia i klinicheskaia farmakologiia, 60(3), 27–29. https://pubmed.ncbi.nlm.nih.gov/9324392/ Bespalov, V. G., Troian, D. N., Petrov, A. S., Morozov, V. G., & Khavinson, V. K.h (1989). Ingibiruiushchiĭ éffekt timogena na razvitie opukholeĭ pishchevoda i predzheludka, indutsirovannykh étilovym éfirom N-nitrozosarkozina u krys [Inhibiting effect of thymogen on the development of tumors of the esophagus and forestomach induced by N-nitrososarcosine ethyl ester in rats]. Eksperimental'naia onkologiia, 11(4), 23–26. https://pubmed.ncbi.nlm.nih.gov/2759010/ Anisimov, V. N., Miretskiĭ, G. I., Morozov, V. G., Pavel'eva, I. A., & Khavinson, V. K.h (1992). Vliianie sinteticheskogo immunomoduliatora timogena na radiatsionnyĭ kantserogenez u krys [The effect of the synthetic immunomodulator thymogen on radiation-induced carcinogenesis in rats]. Voprosy onkologii, 38(4), 451–458. https://pubmed.ncbi.nlm.nih.gov/1300740/ Smirnov, V. S., Petlenko, S. V., & El'tsin, S. S. (2011). Advances in gerontology = Uspekhi gerontologii, 24(2), 278–284. https://pubmed.ncbi.nlm.nih.gov/21957588/ Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
Sermorelin & GHRP-2 Blend (10mg)
Sermorelin is a research peptide made of 29 amino acids that is a truncated version of the full 44-aa length endogenous Growth Hormone-Releasing Hormone (GHRH). Sermorelin is considered the shortest functional analogue that contains the first 29 amino acids, and it is also amidated at the C-terminus. According to research by Clark et al., the peptide appears to retain its affinity to the GHRH receptors found in pituitary cells and activate them.(1) Thus, Sermorelin is considered a GHRH analog. GHRH receptors are the main receptors on pituitary cells that are considered to play a role in the synthesis of growth hormone. Research by Berlanga-Acosta et al. describes GHRP-2 as a fully synthetic hexapeptide, developed from earlier GHRPs such as GHRP-6 and ultimately based on modified enkephalins (endogenous opioid pentapeptides).(2) It is engineered to favor growth hormone release rather than opioid activity, apparently by targeting ghrelin (growth hormone secretagogue) receptors instead of classical opioid receptors. Because GHRP-2 and related GHRPs share this receptor system, they are broadly referred to as growth hormone secretagogues (GHSs). Researchers suggest that by targeting different pituitary receptors with the same potential, peptides like Sermorelin and GHRP-2 may have synergistic actions. Future research should elucidate this more thoroughly. Chemical Makeup Other Known Titles Sermorelin: GRF 1-29 NH2 GHRP-2: pralmorelin Molecular Weight: Sermorelin:93 g/mol GHRP-2:97 g/mol Molecular Formula: Sermorelin: C149H246N44O42S GHRP-2: C45H55N9O6 Research and Clinical Studies Sermorelin & GHRP-2 Actions on Pituitary Cells Sermorelin appears to act primarily at GHRH receptors, which normally respond to endogenous GHRH. Work by Culhane et al. suggests that GHRH analogs may interact with the receptors via G-protein coupling, followed by cAMP production, and downstream growth hormone release. (3) Consequently, the upregulated growth hormone release may interact with growth hormone receptors in a variety of cells, which may synthesize a major anabolic mediator called insulin-like growth factor-1 (IGF-1). By contrast, GHRP-2 is thought to target the ghrelin receptors, which are also known as growth-hormone secretagogue receptors. Specifically, these are the GHS receptors 1a. Research by Yin et al. has deeply investigated these receptors, and they posit that these are seven-transmembrane G-protein-coupled receptors.(4) The interaction may then trigger a chain of intracellular signals starting with an enzyme at the cell membrane called phospholipase C (PLC). PLC cuts a specific membrane fat molecule (PIP₂) into two smaller signaling molecules. One molecule, called IP₃, moves into the fluid inside the cell and may ultimately bind to channels on internal calcium stores, causing Ca²⁺ to be released into the cytoplasm. The other fragment, called DAG, stays in the membrane and helps switch on another enzyme family called protein kinase C (PKC), which adds phosphate groups to selected proteins and thereby changes their activity. In combination, the temporary rise in intracellular calcium and the activation of PKC may activate the genes associated with growth hormone synthesis and also stimulate the release of growth hormone molecules out of the pituitary cells. Sermorelin & GHRP-2 Potential on Somatotroph Growth Hormone Output Vittone et al. explored the potential of Sermorelin on the growth hormone output capacity of pituitary cells and suggest that the peptide may double it.(5) Specifically, the researchers commented that 12-hour mean growth hormone concentration increased from 1.1 ± 0.9 µg/L to 2.2 ± 1.9 µg/L, and the integrated growth hormone secretion over 12 hours. increased from 1114 ± 931 µg·min/L to 2032 ± 1728 µg·min/L. This apparent increase in GH synthesis and release per pulse was accompanied by “no change in GH pulse frequency or in levels of IGF-I, IGFBP-3, or GHBR.” Nevertheless, the authors posited that local, tissue-level IGF-I production in targets such as skeletal muscle cells might still be modulated, even if overall IGF-I remains relatively stable. The researchers also posited that if muscle cells are exposed to the GH peaks induced by Sermorelin, this may be associated with better-supported muscle cell performance. According to further research by Khorram et al., the majority of the increase in GH synthesis may be within the first 2 hours of the pituitary cells being exposed to Sermorelin.(6) The integrated 2-hour GH area observed by the authors apparently rose from about 200-300 to 1,100–1,600 µg·L⁻¹·min (roughly 6-fold). Additionally, this team of researchers also observed an increase in the IGF-1. Mean IGF-I rose apparently by about 27-28%. According to the available research, such as experiments by Bowers et al., GHRP-2 may also upregulate growth hormone synthesis by pituitary cells.(7) Particularly in the case of continuous exposure for 24 hours, the peptide apparently led to an increase from roughly 20–30 µg·L⁻¹·24 h under placebo conditions to about 120–180 µg·L⁻¹·24 h with GHRP-2, implying an approximate 4- to 6-fold rise in growth hormone production. This pattern is compatible with a sustained stimulatory action on growth hormone synthesis by pituitary cells and pulsatile release rather than a brief, desensitizing spike. In the same experiment, IGF-1 concentrations apparently rose from baseline values of about 90–100 µg/L to approximately 150–160 µg/L after the extended 24-hour GHRP-2 exposure. This data suggests that GHRP-2 may increase IGF-1 production by roughly 50–80%, creating a higher steady-state plateau of IGF-1. Sermorelin & GHRP-2 Potential on Other Cells In laboratory settings studied by Chatelain et al., upregulation of IGF-1 by peptides such as Sermorelin may extend beyond pituitary cells and growth hormone dynamics. It might potentially support Leydig cells and their main endocrine function, which is to synthesize testosterone.(8) The increased IGF-1 may act on Leydig cells via the IGF-1 receptor, which is thought to be present on these cells, and has been posited to support their responsiveness to gonadotropins. Experimental data suggest that sustained elevations in growth hormone and IGF-1 may increase LH/hCG receptor density in Leydig cells and may raise hCG-stimulated hormonal output per cell, specifically the hormone testosterone. This pattern is compatible with the possibility that IGF-1 modulates transcription, translation, or membrane trafficking of LH/hCG receptors, thereby amplifying gonadotropin signaling at the Leydig cell surface. In parallel, IGF-1 may also promote expansion of Leydig cell mass and/or support their functional maturation, perhaps through modest mitogenic or differentiation-supporting pathways. However, these mechanisms remain hypothetical and would require targeted verification in controlled laboratory models. Experimental work with GHRP-2 also suggests that this peptide may interact with receptors outside pituitary cells. Specifically, research by Granado et al. suggests that the peptide may modulate liver-associated immune cells during an inflammatory challenge with lipopolysaccharide (LPS).(9) In LPS-stimulated hepatocyte–nonparenchymal cocultures, GHRP-2 apparently reduced TNF-α mRNA and nitrite/nitrate release, which are important inflammatory markers. Researchers like these also tend to express through their research the theory that GHRP-2 may act primarily on nonparenchymal immune cells (such as Kupffer or Kupffer-like macrophages) rather than directly on hepatocytes. Separate lines of research have proposed that GHRP-type peptides may bind CD36 on macrophages, so it is plausible that, in such models, GHRP-2 may signal via CD36 on these immune cells, dampening LPS-driven activation programs that lead to TNF-α and inducible nitric oxide synthase induction. The downstream normalization of nitric oxide and cytokine output may then secondarily interact with neighboring hepatocytes in cell cultures, including their IGF-I expression. Sermorelin & GHRP-2 Synergistic Potential The already mentioned work in experimental pituitary systems by Bowers et al. has explored how GHRP-2 may behave when combined with endogenous GHRH. They observed that simultaneous exposure to GHRP-2 and unmodified GHRH may raise integrated 24-hour growth hormone output from baseline values of roughly 20–30 µg·L⁻¹ to about 238 ± 28 up to 452 ± 106 µg·L⁻¹. These findings correspond to an apparent ~16-fold elevation over baseline GH exposure and more than a twofold increase compared with GHRP-2 alone. Thus, the concurrent activation of the GHS-R1a and the GHRH receptor on pituitary cells may exert synergistic actions to generate a markedly amplified growth hormone secretion in laboratory settings. The researchers also concluded that the “combined GHRP-2 and GHRH drive is more effective than either agonist alone.” Laboratory work by Veldhuis et al., using a similar experimental setting, also points to a potentially synergistic interaction between GHRP-2 and full-length GHRH at the level of pituitary cell cultures. In their experimental models, GHRH alone was estimated to increase growth hormone burst by roughly 20-fold over baseline, whereas GHRP-2 alone was associated with an even larger 47-fold rise. When both secretagogues were present together, the calculated response increased to around 54-fold above saline, which was on the order of 10–15% higher than GHRP-2 alone. This pattern is also compatible with the theory that while each peptide strongly activates somatotroph signaling on its own, combined receptor engagement may provide an additional amplification of growth hormone release. By extension, the GHRH-analog Sermorelin should also exert synergistic potential when combined in experiments at the pituitary-cell level. To confirm this, a small clinical series by Sigalos et al. specifically investigated Sermorelin with GHRP-2 (plus an additional GHRP).(11) According to their data, the combination may drive a substantially stronger IGF-1 response than GHRP-2 alone. Apparently, Sermorelin, GHRP-2, and another GHRP increased IGF-1 from about 160 ng/mL at baseline to roughly 250–265 ng/mL. This is interpreted as roughly a 50–70% rise and a clear upward shift within the reference range. These data points are compatible with the notion that dual-pathway stimulation of pituitary somatotrophs may produce a markedly greater IGF-1 increase than either peptide alone. However, this study is not able to prove superiority because it lacked adequate levels of experimentation. Sermorelin & GHRP-2 blend is available for research and laboratory purposes only. Please review our Terms and Conditions before ordering. References: Clark RG, Robinson IC. Growth induced by pulsatile infusion of an amidated fragment of human growth hormone releasing factor in normal and GHRF-deficient rats. Nature. 1985 Mar 21-27;314(6008):281-3. doi: 10.1038/314281a0. PMID: 2858818. Berlanga-Acosta J, Abreu-Cruz A, Herrera DGB, Mendoza-Marí Y, Rodríguez-Ulloa A, García-Ojalvo A, Falcón-Cama V, Hernández-Bernal F, Beichen Q, Guillén-Nieto G. Synthetic Growth Hormone-Releasing Peptides (GHRPs): A Historical Appraisal of the Evidences Supporting Their Cytoprotective Effects. Clin Med Insights Cardiol. 2017 Mar 2;11:1179546817694558. doi: 10.1177/1179546817694558. PMID: 28469491; PMCID: PMC5392015. Culhane KJ, Liu Y, Cai Y, Yan EC. Transmembrane signal transduction by peptide hormones via family B G protein-coupled receptors. Front Pharmacol. 2015 Nov 5;6:264. doi: 10.3389/fphar.2015.00264. PMID: 26594176; PMCID: PMC4633518. Yin Y, Li Y, Zhang W. The growth hormone secretagogue receptor: its intracellular signaling and regulation. Int J Mol Sci. 2014 Mar 19;15(3):4837-55. doi: 10.3390/ijms15034837. PMID: 24651458; PMCID: PMC3975427. Vittone J, Blackman MR, Busby-Whitehead J, Tsiao C, Stewart KJ, Tobin J, Stevens T, Bellantoni MF, Rogers MA, Baumann G, Roth J, Harman SM, Spencer RG. Effects of single nightly injections of growth hormone-releasing hormone (GHRH 1-29) in healthy elderly men. Metabolism. 1997 Jan;46(1):89-96. doi: 10.1016/s0026-0495(97)90174-8. PMID: 9005976. Khorram O, Laughlin GA, Yen SS. Endocrine and metabolic effects of long-term administration of [Nle27]growth hormone-releasing hormone-(1-29)-NH2 in age-advanced men and women. J Clin Endocrinol Metab. 1997 May;82(5):1472-9. doi: 10.1210/jcem.82.5.3943. PMID: 9141536. Bowers, C. Y., Granda, R., Mohan, S., Kuipers, J., Baylink, D., & Veldhuis, J. D. (2004). Sustained elevation of pulsatile growth hormone (GH) secretion and insulin-like growth factor I (IGF-I), IGF-binding protein-3 (IGFBP-3), and IGFBP-5 concentrations during 30-day continuous subcutaneous infusion of GH-releasing peptide-2 in older men and women. The Journal of clinical endocrinology and metabolism, 89(5), 2290–2300. https://doi.org/10.1210/jc.2003-031799 Chatelain PG, Sanchez P, Saez JM. Growth hormone and insulin-like growth factor I treatment increase testicular luteinizing hormone receptors and steroidogenic responsiveness of growth hormone deficient dwarf mice. Endocrinology. 1991 Apr;128(4):1857-62. doi: 10.1210/endo-128-4-1857. PMID: 2004605. Granado M, Martín AI, López-Menduiña M, López-Calderón A, Villanúa MA. GH-releasing peptide-2 administration prevents liver inflammatory response in endotoxemia. Am J Physiol Endocrinol Metab. 2008 Jan;294(1):E131-41. doi: 10.1152/ajpendo.00308.2007. Epub 2007 Nov 6. PMID: 17986630. Veldhuis JD, Keenan DM. Secretagogues govern GH secretory-burst waveform and mass in healthy eugonadal and short-term hypogonadal men. Eur J Endocrinol. 2008 Nov;159(5):547-54. doi: 10.1530/EJE-08-0414. Epub 2008 Aug 14. Erratum in: Eur J Endocrinol. 2008 Dec;159(6):841. PMID: 18703567; PMCID: PMC2680123. Sigalos JT, Pastuszak AW, Allison A, Ohlander SJ, Herati A, Lindgren MC, Lipshultz LI. Growth Hormone Secretagogue Treatment in Hypogonadal Men Raises Serum Insulin-Like Growth Factor-1 Levels. Am J Mens Health. 2017 Nov;11(6):1752-1757. doi: 10.1177/1557988317718662. Epub 2017 Aug 22. PMID: 28830317; PMCID: PMC5675260. Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
Chonluten (20mg)
Chonluten, also known as EDG tripeptide or T-34, is a tripeptide that may potentially regulate the physiological processes of the respiratory system by influencing inflammation and proliferation. It may potentially restore mechanisms of anabolism and catabolism, critical to functional tissues. Chonluten is a peptide complex containing glycine, glutamine, and asparagine, which is considered to normalize the performance of bronchial mucous membrane cells.(1) Chonluten has been primarily researched for its potential to normalize the impact on target organs by replacing or supporting the activity of substances secreted by these morphological structures through immunomodulation. It may possibly increase the lifespan of mesenchymal stem cells (MCS) and possibly induce molecular mechanisms that contrast senescence. Chonluten appears to be organ-specific, with its primary potential exhibited in lung tissues, possibly extending action in the gastrointestinal tract.(2) Chonluten may revitalize, regulate, and otherwise provide favorable actions on the airway and bronchial mucosa. Chemical Makeup(3) Molecular Formula: C11H17N3O8 Molecular Weight: 319.27 g/mol Structure: 4S)-4-amino-5-[[(2S)-3-carboxy-1-(carboxymethyl amino)-1-oxopropan-2-yl]amino]-5-oxopentanoic acid Other Known Titles: Glu-asp-gly, Glutamyl-aspartyl-glycine, H-Glu-asp-gly-OH, T-34 tripeptide Research and Clinical Studies Chonluten Peptide and Inflammation Reduction As lung capacity reduces, researchers suggest Chonluten may decrease the rate of cell death while encouraging proliferative activity via protection of the bronchial lining. (1) The bronchial inner lining is a barrier between the external environment and internal structures. Different inflammatory conditions may affect this inner lining and change mucus production and the structure of the cells’ extracellular matrix. Chonluten's proposed mechanisms of action may help reduce levels of inflammation within the lungs. One such potential mechanism of action may be the initiation of phosphorylation in STAT molecules, especially STAT1, within immune cells called macrophage cells. STAT stands for "Signal Transducer and Activator of Transcription.” These molecules appear to be messengers inside the cells, mediating signals and passing them to the cellular nucleus. Thus, STAT1 works like a switch that turns on genes, and it might work together with other proteins to send immune signal messages into the macrophage cell's nucleus, ultimately regulating this type of immune cell and reducing inflammation. The researchers also theorized that Chonluten may potentially decrease the activation of STAT3, another important protein that may act like a gene switch. STAT3 is involved in quick immune responses and might help control the gene for IL-6 (interleukin-6), an important immune system protein during inflammation. By affecting STAT3, Chonluten might change how IL-6 works, which could help reduce inflammation. Further, the researchers suggest Chonluten might exhibit some capacity to reduce levels of IL-6, TNF (tumor necrosis factor), and IL-17 in immune cells triggered by bacterial and other foreign substances. IL-6, TNF, and IL-17 are all proteins that scientists consider to cause inflammation and help regulate the immune system. Lowering the levels of these proteins may help calm inflammation in these activated immune cells. The scientists commented that the peptide apparently “inhibited in vitro tumor necrosis factor (TNF) production of monocytes exposed to pro-inflammatory bacterial lipopolysaccharide (LPS). The low TNF release by monocytes is linked to a documented mechanism of TNF tolerance, promoting attenuation of inflammatory action." Chonluten might also reduce the sticking process between the inner lining of blood vessels and immune cells. This was first posited by researchers who observed Chonluten mixed with endothelial cells (cells lining blood vessels) in experiments. By changing how these cells stick to each other, Chonluten may potentially affect how immune cells move and travel around the organism, which may be important in controlling inflammation and immune reactions.(1) Chonluten Peptide and Gastrointestinal Tract Tissues Chonluten's suggested impact on the gastrointestinal tract is reportedly similar to that in the lungs, with studies positing its potential to reduce inflammation and prevent the prevalence of vascular changes that induce inflammatory diseases. For example, Chonluten might help repair cells in the stomach and intestinal tissues. It is posited to do this by controlling the activity of genes linked to antioxidant enzymes like superoxide dismutase (SOD). Research on Chonluten suggests that it might normalize these genes, helping to balance antioxidant defenses in the stomach lining. This might reduce oxidative stress, which harms cells, and encourage cell repair. It is also believed that Chonluten may reduce inflammation by affecting inflammation-related genes, such as TNF-α and cyclooxygenase-2 (Cox-2). By lowering the activity of these inflammation-causing substances, Chonluten might help control stomach tissue inflammation, aiding in cell repair. Additionally, Chonluten may promote new tissue growth, important for healing damaged areas. It might encourage the multiplication of fibroblasts, which are cells that help in tissue repair and the growth of new blood vessels in the healing tissue. It may also help repair damaged stomach lining by stimulating the growth of epithelial cells, which could lead to the recovery of damaged and ulcerated tissues. Furthermore, Chonluten may reduce excessive cell death (apoptosis) in the stomach lining. It is thought to possibly regulate the expression of heat shock protein 70 (HSP70), which protects cells from triggers that cause apoptosis. By controlling HSP70, Chonluten may possibly prevent excess cell death and promote the survival and repair of gastrointestinal tract tissues.(2) Chonluten Peptide and Gene Expression Short peptides, such as Chonluten, have been researched in the context of certain modes of DNA expression, such as DNA methylation.(4)(5) Research suggests that “Short peptides, consisting of 2-7 amino acid residues, can penetrate into the nuclei and nucleoli of cells and interact with the nucleosome, the histone proteins, and both single- and double-stranded DNA. DNA-peptide interactions, including sequence recognition in gene promoters, are important for template-directed synthetic reactions, replication, transcription, and reparation. Peptides can regulate the status of DNA methylation, which is an epigenetic mechanism for the activation or repression of genes in both the normal condition, as well as in cases of pathology and senescence.”(4) Chonluten Peptide and the Immune System Research studies suggest that Chonluten may regulate the immune system, stimulating or suppressing it to respond to advancing conditions. Chonluten's possible mechanisms of action have been suggested to be mediated by many genes, including heat shock protein, gene HSP70, SOD, c-Fos, antioxidative system genes, and TNF-alpha. The regulation of such genes may result in anti-inflammatory impacts, particularly c-Fos—a protein bioregulator of cell differentiation, survival, and proliferation that is activated in response to hypoxia and cellular damage. Although c-Fos may induce the growth of new blood vessels and cell proliferation locally in response to an injury, progressive expression might result in thickened bronchial mucosa or cancer.(2) Chonluten Peptide and Aerobic Activity Research studies have grappled with the role of Chonluten peptide in various aerobic studies: “Studies have [suggested] that several bioactive peptides elicit strongly upregulating effects on muscle protein synthesis or increase muscular strength and recovery [...] Besides positive effects on [contractile] strength and recovery, recent investigations found that hydrolyzed proteins might also influence endurance performance and metabolism.”(6) Further research indicates that the Chonluten tripeptide might reduce stress hormone secretion and potentially improve the organism’s tolerance to low oxygen conditions. This suggests that the Chonluten tripeptide could help the lung and muscle tissues work better when insufficient oxygen exists. For example, researchers share that the Chonluten tripeptide may possibly exert a protective effect against low oxygen stress, which might stem from the peptide’s potential to control the activity of certain genes. These genes may include the c-Fos gene, which is involved in cell growth and survival; the heat shock protein gene HSP70, which might protect cells from low oxygen stress; genes that make enzymes in internal antioxidant systems, like SOD and COX-2, which are considered to help protect against oxidative damage; and the tumor necrosis factor gene TNF-α, which is believed to be important in inflammation and immune response. These findings suggest that the Chonluten tripeptide might potentially influence various biological processes, contributing to what seems to be its effect in protecting against low oxygen stress. (7) Chonluten peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References Avolio F, Martinotti S, Khavinson VK, Esposito JE, Giambuzzi G, Marino A, Mironova E, Pulcini R, Robuffo I, Bologna G, Simeone P, Lanuti P, Guarnieri S, Trofimova S, Procopio AD, Toniato E. Peptides Regulating Proliferative Activity and Inflammatory Pathways in the Monocyte/Macrophage THP-1 Cell Line. Int J Mol Sci. 2022 Mar 25;23(7):3607 V. K. Khavinson, N. S. Lin’kova, A. V. Dudkov, V. O. Polyakova, and I. M. Kvetnoi, “Peptidergic regulation of expression of genes encoding antioxidant and anti-inflammatory proteins,” Bull. Exp. Biol. Med., vol. 152, no. 5, pp. 615–618, Mar. 2012, DOI: 10.1007/s10517-012-1590-2 PubChem [Internet]. Bethesda (MD): National Library of Medicine (US), National Center for Biotechnology Information; 2004-. PubChem Compound Summary for CID 194641, Glutamyl-aspartyl-glycine; [cited 2024 Feb. 20]. Available from: https://pubchem.ncbi.nlm.nih.gov/compound/Glutamyl-aspartyl-glycine Khavinson VK, Popovich IG, Linkova NS, Mironova ES, Ilina AR. Peptide Regulation of Gene Expression: A Systematic Review. Molecules. 2021 Nov 22;26(22):7053 Khavinson VK, Lin'kova NS, Tarnovskaya SI. Short Peptides Regulate Gene Expression. Bull Exp Biol Med. 2016 Dec;162(2):288-292 König D, Kohl J, Jerger S, Centner C. Potential Relevance of Bioactive Peptides in Sports Nutrition. Nutrients. 2021 Nov 10;13(11):3997. DOI: 10.3390/nu13113997 Khavinson, V., Linkova, N., Dyatlova, A., Kuznik, B., & Umnov, R. (2020). Peptides: Prospects for Use in the Treatment of COVID-19. Molecules (Basel, Switzerland), 25(19), 4389. https://doi.org/10.3390/molecules25194389 Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.