Vialox, also termed Pentapeptide-3V, is a peptide developed to induce partial muscle paralysis, potentially resulting in a decreased prevalence of wrinkles and creases forming along skin structures.^[1]

Pentapeptide-3V may prevent muscle contraction by exhibiting a curare-like effect at the neuromuscular junction, disallowing the nervous system signals from reaching the muscles.

Pentapeptide-3V is of primary interest because of its influential ability to communicate between muscles and nerves.

Pentapeptide-3V may affect the signal transmission between nerves and muscles. In normal conditions, signals are transmitted following the release of acetylcholine from its axon by nerves. Contraction occurs following the conduction of acetylcholine across the neuromuscular junction to bind to a receptor on the muscle. Pentapeptide-3V appears to halt contraction by binding to the AChR.^[3] By doing this, it may block acetylcholine from binding. This may result in a reduced amount of acetylcholine binding and reduced strength and number of muscle contractions.

Acetylcholine appears to bind to a muscle receptor, limiting sodium ion release at the neuromuscular junction. Depolarization occurs, resulting in electrical pulses that cause wrinkles and muscle contraction. By binding to AChR, Pentapeptide-3V may potentially inhibit this process. When Pentapeptide-3V binds to AChR, it may inhibit acetylcholine binding.

Pentapeptide-3V appears to only affect peripheral AChRs and may not potentially affect central neuronal receptors, unlike the other nicotinic acetylcholine receptor antagonists. This suggests that Pentapeptide-3V only acts on the neuromuscular junction.

The overall result of Pentapeptide-3V activity is suggested to be a reduction in acetylcholine binding following the reduction in the frequency and intensity of muscular contractions.^[4]

Pentapeptide-3V may potentially reduce average skin roughness by 11% and relief by 8%. Because relief is proportional to wrinkle size, Vialox can reduce wrinkles by an average of 8%. These are in approximately 60% and 47% of the animal subjects examined. According to Reddy et al. “this product is effective in smoothing … wrinkles and provides an immediate tightening effect to the skin.”^[5]

Pentapeptide-3V, a protein composed of lysine, threonine, and serine, is considered an abundant protein in skin collagen. It appears to act directly on the dermis to stimulate collagen production. Ancillary compounds examined in studies, such as Vitamin A, according to research conducted by specialists in the Department of Dermatology, suggest that Pentapeptide-3V may potentially increase collagen growth, improving skin compaction. Pentapeptide-3V may stimulate collagen production in the skin, reversing aging and minimizing wrinkles. Vialox may also improve the production of melanin to act in mitigatory fashion against UV radiation.

 

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

 

References

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1. Servent, D. et al. Only Snake Curaremimetic Toxins with a Fifth Disulfide Bond Have High Affinity for the Neuronal α7 Nicotinic Receptor. J. Biol. Chem. 272, 24279–24286 (1997) DOI: 10.1074/jbc.272.39.24279
2. Zhmak, M. N., Utkin, Y. N., Andreeva, T. V., Kudryavtsev, D. S., Kryukova, E. V., Tsetlin, V. I., … & Shelukhina, I. V. E. (2017). U.S. Patent No. 9,550,808. Washington, DC: U.S. Patent and Trademark Office.
3. Gupta, V. K. Biotechnology of Bioactive Compounds: Sources and Applications. (John Wiley & Sons, 2015)
4. Reddy, B. Y., Jow, T., & Hantash, B. M. (2012). Bioactive oligopeptides in dermatology: Part II. Experimental dermatology, 21(8), 569-575.

Syn-Coll, also known as Palmitoyl Tripeptide-5 or Tripeptide-5, is a peptide that researchers suggest may act to increase the production of Type I and Type III collagen while possibly also inhibiting its degradation. Palmitoyl Tripeptide-5 is suggested to act by activating transforming growth factor-𝛃.^[1] Collagen type I is present in the bones, muscles, and skin. Type III collagen, on the other hand, is present in the skin, vascular system, and lungs. By increasing Type I and Type III collagen, Syn-Coll may potentially promote tissue repair processes as well as contributing to structural support for the extracellular matrix of the skin.

Fibroblasts are considered to be among the most commonly occurring cells in the skin. The main function of these cells appears to be the production collagen proteins. The number of active fibroblasts and levels of collagen declines naturally, potentially leading to increasing instances of creasing across the skin surface. Palmitoyl Tripeptide-5 appears to function similarly to Thrombospodin-1 to stimulate transforming growth factor-induced collagen degradation.

 

Functions of Palmitoyl Tripeptide-5

TSP-1 is a naturally occurring peptide that appears to increase TGF-𝛃 activities. Palmitoyl Tripeptide-5 appears to exhibit the same characteristics as TSP-1, increasing Type I and III collagen levels in the dermal (skin) fibroblasts.^[2] The researchers noted that “Investigator assessments of both periocular and perioral wrinkles showed statistically significant improvements over Baseline within minutes of initial application; these positive findings continued to improve through Months 1 and 3.” Experimental results suggest that Syn-Coll increases Type I and III collagen levels by 2-3 folds above the normal levels.^[3]

TSP-1 is considered to be an extracellular matrix (ECM) protein. It appears to cohabit with collagen and elastin in the skin. A specific part of TSP-1 is harvested for use in Palmitoyl Tripeptide-5 production. This part stimulates latent TGF-𝛃. Just like TSP-1, Syn-Coll may function to enhance tissue repair. It appears active in the post-natal development of skin structures.^[4]

Palmitoyl Tripeptide-5 may also potentially deactivate matrix metalloproteinases I and III (MMP1 and MMP3). Matrix metalloproteinases are enzymes that act to degrade collagen. These enzymes may be beneficial, as they recycle collagen following cell aging, but they have been suggested to hike in conditions such as inflammation to abnormal levels.

By inhibiting MMP1 and MMP3 activity, Palmitoyl Tripeptide-5 may potentially help to prevent collagen breakdown. These hypotheses suggest that Syn-Coll may promote Type I and Type III collagen formation and inhibit collagen breakdown by the abovementioned enzymes.

In terms of wrinkle reduction, Syn-Coll has been suggested to be approximately 3.5x more effective than a placebo. According to scientists, Palmitoyl Tripeptide-5 is 60% more effective than Palmitoyl Pentapeptide.^[5]  Palmitoyl Tripeptide-5 has been suggested to alter the effects of photo-aging damage. Syn-Coll may also rarefy pores, potentially diminishing inconsistencies in skin texture and increasing skin elasticity and firmness. Palmitoyl Tripeptide-5 is considered to be cold-processible.

 

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

 

References

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1. Thorsen, M., Yde, B., Pedersen, U., Clauden, K. & Lawesson, S.-O. Studies on amino acids and peptides-V. Tetrahedron 39, 3429–3435 (1983).https://doi.org/10.1016/S0040-4020(01)91596-0
2. Trookman, N. S., Rizer, R. L., Ford, R., Ho, E. & Gotz, V. Immediate and Long-term Clinical Benefits of a Treatment for Facial Lines and Wrinkles. J. Clin. Aesthetic Dermatol. 2, 38–43 (2009).
3. Varga, J., Rosenbloom, J. & Jimenez, S. A. Transforming growth factor beta (TGF beta) causes a persistent increase in steady-state amounts of type I and type III collagen and fibronectin mRNAs in normal human dermal fibroblasts. Biochem. J. 247, 597–604 (1987).
4. Murphy-Ullrich, J. E. & Poczatek, M. Activation of latent TGF-beta by thrombospondin-1: mechanisms and physiology. Cytokine Growth Factor Rev. 11, 59–69 (2000).
5. Bucay, V. W. & Day, D. Adjunctive Skin Care of the Brow and Periorbital Region. Clin. Plast. Surg. 40, 225–236 (2013).

Pal AHK is a peptide also termed Palmitoyl Tripeptide-3. Experiments on Pal AHK suggest that the peptide can activate fibroblast production through its interaction with transforming growth factor-𝛽 (TGF-𝛽). Due to the peptide’s potential to enhance collagen production and reduce creasing across the skin structure, it has been widely researched.

 

Pal AHK Peptide Overview

Pal AHK peptide is associated with palmitoyl fatty acid molecules. This fatty acid feature appears to make AHK soluble in fats. Due to this, the rate at which Pal AHK peptide may potentially penetrate the skin increases and may increase its absorption by cells. Pal AHK present in the skin may activate the production of TGF-𝛽.

The activation of fibroblast production in the skin by Palmitoyl Tripeptide-3 may potentially increase the extracellular matrix (ECM) synthesis in the skin.^[2] The extracellular matrix (ECM) is a complex network of minerals and extracellular macromolecules. It is dominated by enzymes, elastin, glycoproteins, collagens, and hydroxyapatite, considered responsible for providing biochemical and structural support to the surrounding cells. By increasing the extracellular matrix (ECM) synthesis in the cell, Pal AHK peptide may possibly increase the production of ECM components, increasing cell-to-cell attachment and communication, cell growth, and cell movement.^[3]

Experiments suggest that Pal AHK peptide may possibly modulate the synthesis of vascular endothelial growth factor (VEGF). Vascular endothelial growth factor (VEGF) is a signaling molecule activated in the production of new blood vessels.^[4] The scientists also explain that “Vascular endothelial growth factor (VEGF) is an endothelial cell mitogen and permeability factor that is potently angiogenic.” By enhancing vascular endothelial growth factors, Pal AHK may possibly boost the production of new blood vessels in the skin. Increased vascular endothelial growth factor (VEGF) by Palmitoyl Tripeptide-3 may allow for increased blood supply to the skin.

The vascular endothelial growth factor (VEGF) may prevent disease conditions such as macular degeneration, diabetes, and even cancer, though research in this area is ongoing. The vascular endothelial growth factor (VEGF) is an angiogenic factor suggested to influence angiogenesis by paving the way for endothelial cell proliferation, migration, and permeability. By increasing the production of VEGF, Pal AHK peptide may possibly enhance the prevention of cancer, macular degeneration, and diabetes while potentially preventing the onset of possible cardiac and cardiac-related diseases.

The production of new blood vessels may improve wound healing by depositing the injury site with collagen. This is considered to be due to the vascular endothelial growth factor (VEGF). Therefore, increasing VEGF by Palmitoyl Tripeptide-3 may increase the wound healing process. It is vital to note that in a laboratory setting, the vascular endothelial growth factor (VEGF) may exhibit mitogenic, chemotactic, and permeability action. These may be impactful in the regeneration and repair of non-healing wounds following diabetes and artery occlusive diseases.

Palmitoyl Tripeptide-3 may potentially increase VEGF production and contribute to modest visual improvement—averaging about two lines of vision. When Palmitoyl is added to AHK, it may potentially increase the penetrating rate of Pal AHK peptide in the cell membrane. Thus, increasing collagen production.

Pal AHK peptide has been suggested to minimize muscle contractions, therefore, decreasing and inhibiting the onset of wrinkling along the skin surface.

Oxidative stress (free-radical attack) is a considered cause of reduced follicle growth and loss. The peptide may potentially decrease follicle loss and enhance growth by decreasing oxidative stress. Due to the reduction of oxidative stress by Palmitoyl Tripeptide-3, dihydrotestosterone formation in follicles may increase.^[5] The scientists note that “Animal studies indicate that palmitoyl tripeptide-3/5 may increase collagen synthesis… Studies [suggest] that palmitoyl tripeptide-3/5 can prevent collagen breakdown by interfering with MMP1 and MMP3 collagen degradation.” The inhibition of oxidative stress by Pal AHK peptide may potentially be achieved by boosting superoxide dismutase production. As a result, it may mitigate the damaging action of oxidative stress.

 

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

 

References

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1. Åubkowska, B., Grobelna, B. & Maćkiewicz, Z. The use of synthetic polypeptides in cosmetics. Copernic. Lett. 1, 75 (2010).
2. Gorouhi, F. & Maibach, H. I. Role of peptides in preventing or treating aged skin. Int. J. Cosmet. Sci. 31, 327–345 (2009).
3. Lourith, N. & Kanlayavattanakul, M. Biopolymeric agents for skin wrinkle treatment. J. Cosmet. Laser Ther. 18, 301–310 (2016).
4. Nör JE, Christensen J, Mooney DJ, Polverini PJ. Vascular endothelial growth factor (VEGF)-mediated angiogenesis is associated with enhanced endothelial cell survival and induction of Bcl-2 expression. Am J Pathol. 1999;154(2):375-384. doi:10.1016/S0002-9440(10)65284-4.

Decapeptide-12 is considered to be an anti-tyrosinase peptide. The peptide has been suggested to inhibit the activities of tyrosinase, an enzyme that catalyzes the production of melanin and other pigments.^[1] According to research “tyrosinase activity and melanin production … is controlled primarily by a post-translational regulation of pre-existing enzyme and not by regulating tyrosinase gene activity.”

Tyrosinase may be present in plant and animal cells, where it appears to aid the catalyzation of melanin. The peptide has also been suggested to aid in dihydroxyphenylalanine catalysis. Decapeptide-12 may potentially foster the catalysis of the first two steps in the biochemical synthesis of melanin and is expressed by melanocytes. Notably, tyrosinase may be in melanosomes-synthesized in the melanocytes.

Type I oculocutaneous a lack of tyrosinase has been linked to albinism. In contrast, skin hyperpigmentation has been linked to melanin synthesis. It may also be caused by a mutation that causes tyrosinase to become overactive. Decapeptide-12, considered to be a tyrosinase inhibitor, is of interest to the researchers due to its potential to improve the function of the enzyme cascade of pigment production.

Decapeptide-12 appears to inhibit tyrosinase activities by reversibly binding to tyrosinase in several pigment-producing cells.^[2] The peptide may potentially prevent the oxidation of phenols by tyrosinase, the first step in melanin production. Tyrosinase is primarily found in melanosomes—unique parts within cells that produce pigments. Tyrosinase varies in structure according to species or even in closely related species.

Tyrosinase is also considered to aid the oxidation of phenolic compounds in fruits and vegetables to quinones (i.e., what turns potato black after it is sliced). This conversion may cause taste and odor alterations in the fruits and vegetables. This conversion may cause some kinds of proteins to be harder to digest and potentially decrease the nutritional value of the food. Decapeptide-12 has been researched in conjunction with the preservative potential that may be induced in fruits and vegetables when tyrosinase activity is inhibited.

Tyrosinase peptide inhibitors, possibly Decapeptide-12, are considered potential insecticides as they appear to inhibit tyrosinase’s activities in insects. Tyrosinase may act to heal wounds, parasite encapsulation, and develop an insect’s exoskeleton. Therefore, the inhibition of tyrosinase may hamper its activities in insects leading to an insect’s death.

Decapeptide-12 appears to potentially reduce skin pigmentation, according to research in animal models aimed at determining its action in research models of melasma (photodamage). According to studies, approximately 40% of the research models in the experiment developed a 100% decrement of pigmentation-hyperpigmentation. About 15% of the models of grade 3 photodamage exhibited an apparent turnaround and moved into grade 1 photodamage. Research models of severe photodamage (photodamage grade 4) were observed to have only minor repairs, lowering them to photodamage grade 3.^[3] The exposure to Decapeptide-12 peptide to nearly all research models of Melasma (photodamage) appeared to result in changes to skin tone.^[4]

According to research, Decapeptide-12 may be 17 times greater in impact than control hyperpigmentation procedures.^[5] Studies report that “This inhibition partially depended on whether L-dopa or L-tyrosine was the substrate, suggesting that tyrosinase may contain contains two distinct catalytic sites.” Including hydroquinone, with no evidence of melanocyte damage. Research studies in cultured melanocytes for more than 7 days suggested a 27% – 43% decrease in melanin content.

Decapeptide-12 appears to synergize with glycolic acid to remove the dead stratum corneum layers concentrated with hyperpigmented cells.  Decapeptide-12 may potentially protect skin cells from hyperpigmentation. This may be possible through preventing UV rays from reaching the skin’s sensitive layers and shielding the skin from any harmful interaction of UV rays with melanocytes, possibly preventing the spread of new damage.

 

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

 

References

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1. Iozumi, K., Hoganson, G. E., Pennella, R., Everett, M. A. & Fuller, B. B. Role of tyrosinase as the determinant of pigmentation in cultured human melanocytes. J. Invest. Dermatol. 100, 806–811 (1993).
2. Chen J, Bian J, Hantash BM, et al. Enhanced skin retention and permeation of a novel peptide via structural modification, chemical enhancement, and microneedles. Int J Pharm. 2021;606:120868. doi:10.1016/j.ijpharm.2021.120868
3. Kassim, A. T., Hussain, M. & Goldberg, D. J. Open-label evaluation of the skin-brightening efficacy of a skin-brightening system using decapeptide-12. J. Cosmet. Laser Ther. Off. Publ. Eur. Soc. Laser Dermatol. 14, 117–121 (2012).
4. Hantash, B. M. & Jimenez, F. A split-face, double-blind, randomized and placebo-controlled pilot evaluation of a novel oligopeptide for the treatment of recalcitrant melasma. J. Drugs Dermatol. JDD 8, 732–735 (2009).
5. Abu Ubeid, A., Zhao, L., Wang, Y. & Hantash, B. M. Short-sequence oligopeptides with inhibitory activity against mushroom and human tyrosinase. J. Invest. Dermatol. 129, 2242–2249 (2009)

Livagen is classified by scientists as a potential peptide bioregulator of the liver, GI tract, and immune system. Livagen peptide has been suggested to act on the DNA and gene expression patterns. The gene-activating potential of Livagen on the immune system and GI tract may stem from certain cell aging prevention characteristics of the peptide.

Livagen peptide has been suggested to potentially modulate Chromatin, and thereby impact immune system function. Due to DNA packing, DNA in eukaryotes may reduce to roughly 100,000. DNA is a double helix protein wrapped by histone proteins, which may combine to form chromatin structures. The chromatin structure may subsequently condense to form chromosomes.^[2] Researchers suggest that “Livagen causes de-heterochromatinization (activation) of chromatin, which is realized via modification of heterochromatin and heterochromatinized regions.”

Livagen peptide may potentially stimulate chromatin decondensation by activating multiple genes in lymphocytes, according to research. This mechanism may promote the activation of silent genes, such as ribosomal genes, which may potentially boost protein synthesis and cell activity.^[3] During the investigation, a comparison of Livagen, Epithalon, and Vilon was made. Livagen peptide was suggested to exhibit four impacts on lymphocytes, according to the results. Unpacking chromatin was one among them, as well as decondensation, reactivation of ribosomal genes to activate synthetic processes, and the changing the expression of genes may then occur.

B cells, T cells, and natural killer cells are all types of lymphocytes. T cells appear to produce antibodies specific to cells infected with viruses, bacteria, or malignant cells, whereas B cells appear to produce antiviral and antibacterial antibodies. T cells may produce cytokines that influence immune responses and inflammation.

Livagen peptide may potentially influence pain perception. Enkephalins are peptides that are suggested control nociception. They attach to mu and delta-opioid receptors and may potentially transmit pain signals. When Mu receptors, which bind to morphine, are triggered, they may lower pain, blood pressure, and awareness. Delta receptors may alleviate pain and may be involved in opiate-induced respiratory depression.^[4]According to Livagen research, the peptide may block enkephalin-degrading enzyme activity in the blood, causing a rise in natural painkiller levels.

Livagen peptide may interact with the heart muscle. According to research, chromatin dysregulation may be one of the pathogenic components of  hypertrophic cardiomyopathy (HCM) and atherosclerosis.^[5] The scientists suggest that “The peptide bioregulator Livagen could induce reactivation (deheterochromatinization) of chromatin to modify heterochromatinized chromosomal regions in cultured lymphocytes.” Scientists believe that genes produced by chromatin decondensation in lymphocytes might minimize the long-term consequences of several forms of heart disease. Livagen peptide may potentially perform this function. In research models of hypertrophic cardiomyopathy (HCM), altered lymphocyte gene expression might minimize scarring and inflammation.^[6]

Livagen may impact the gastrointestinal tract. According to the Livagen peptide study, the peptide might increase GI tract vagal nerve signaling and change levels of prostaglandins and mucosal nitric oxide. This may lead to gastroprotection, possibly managing diarrhea, symptoms, and inflammatory bowel disease.^[7]

 

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

 

References

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1. Lezhava T. A. (2001). Funktsional’nye osobennosti khromosom cheloveka i starenie [Human chromosome functional characteristics and aging]. Advances in gerontology = Uspekhi gerontologii, 8, 34–43.
2. Khavinson, V. K.h, Lezhava, T. A., Monaselidze, J. G., Dzhokhadze, T. A., Dvalishvili, N. A., Bablishvili, N. K., & Ryadnova, I. Y. (2002). Effects of Livagen peptide on chromatin activation in lymphocytes from old people. Bulletin of experimental biology and medicine, 134(4), 389–392. doi: 10.1023/a:1021924702103.
3. Lezhava, T., Monaselidze, J., Kadotani, T., Dvalishvili, N., & Buadze, T. (2006). Anti-aging peptide bioregulators induce reactivation of chromatin. Georgian medical news, (133), 111–115.
4. Kost, N. V., Sokolov, O. I.u, Gabaeva, M. V., Zolotarev, I.uA., Malinin, V. V., & Khavinson, V. K.h (2003). Vliianie novykh peptidnykh bioreguliatorov livagena i épitalona na énkefalindegradiruiushchie fermenty syvorotki krovi cheloveka [Effect of new peptide bioregulators livagen and epitalon on enkephalin-degrading enzymes in human serum]. Izvestiia Akademii nauk. Seriia biologicheskaia, (4), 427–429.
5. Lezhava, T., Monaselidze, J., Kadotani, T., Dvalishvili, N., & Buadze, T. (2006). Anti-aging peptide bioregulators induce reactivation of chromatin. Georgian medical news, (133), 111–115.
6. Dzhokhadze, T. A., Buadze, T. Z.h, Gaĭozishvili, M. N., Rogava, M. A., & Lazhava, T. A. (2013). Georgian medical news, (225), 94–97.
7. Gyires, K., & Rónai, A. Z. (2001). Supraspinal delta- and mu-opioid receptors mediate gastric mucosal protection in the rat. The Journal of pharmacology and experimental therapeutics, 297(3), 1010–1015.

According to a preliminary rodent study, Thymalin peptide may potentially complement pulsed laser radiation for mitigating the proliferation of cancer cells in certain subtypes of cancer.^[1] Thymalin may potentially increase antibody-producing cells in the spleen. Nonathymulin peptide has been suggested in studies to have tumor mitigating characteristics, with one study reporting tumor development mitigation in almost 80% of instances and decreasing tumor size in nearly half of the animal research models examined.^[2]  Thymalin peptide combined with plasmapheresis may potentially be more effective in combating chronic lympholeukemia.^[3] Furthermore, it might develop hematological compensation than traditional chemotherapy compounds and procedures, in addition to possible improvement in lymphoid function.^[4]

 

Thymalin Peptide and Immune Function

Thymalin peptide may potentially affect cellular immunity, modifying lymphocyte subpopulation levels, influencing T-cell development, and modulating natural killer (NK) cell activity, according to research.^[5] Nonathymulin peptide exposure may possibly correct the immune system and improve T-lymphocyte proliferation in research models of diabetic retinopathy, resulting in less inflammation and slower disease progression rates.^[6] This might apply to chronic immunological deficiency/immune HIV dysregulation. Thymalin, in combination with HAART, may repair immune system damage and increase CD4 + T-cell counts. Research is ongoing to see whether Thymalin may interact with HIV vaccinations to boost immunization responses. Thymalin peptide exposure in mice without the thyroid gland appeared to have reversed or protected the animals from weight loss and cell growth.

 

Thymalin Peptide and Kidney Diseases

Nonathymulin peptide exposure has been suggested in research to potentially mitigate inflammatory kidney disease, such as chronic glomerulonephritis. Research is ongoing.

 

Thymalin and the Circadian-Rhythm

Circadian rhythm disruptions may be due to alterations in thymic components and cellular and humoral immunity, according to research. Changes in circadian rhythm, according to scientists, might affect thymic function, leading to immune system suppression. Thymalin peptide, on the other hand, may not regulate circadian rhythm. However, it might reset alterations in immunological insufficiency induced by variations in sleep-wake cycles.

 

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

 

References

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1. Kozlov, A. P., & Moskalik, K. G. (1980). Pulsed laser radiation therapy of skin tumors. Cancer, 46(10), 2172–2178. doi:10.1002/1097-0142(19801115)46:10‹2172::aid-cncr2820461013›3.0.co;2-l.
2. Zhukova, G. V., Schikhlyarova, A. I., Barteneva, T. A., Shevchenko, A. N., & Zakharyuta, F. M. (2018). Effect of Thymalin on the Tumor and Thymus under Conditions of Activation Therapy In Vivo. Bulletin of experimental biology and medicine, 165(1), 80–83. doi:10.1007/s10517-018-4104-z.
3. Tretiak, N. N., Babenko, T. F., Gaĭdukova, S. N., Zverkova, A. S., & Beschastnaia, S. P. (1998). Effektivnost’ primeneniia timalina i plazmafereza v kompleksnom lechenii bol’nykh khronicheskim limfoleĭkozom [The efficacy of using thymalin and plasmapheresis in the combined treatment of patients with chronic lympholeukemia]. Likars’ka sprava, (2), 93–96.
4. Babenko, T. F., Antonenko, V. T., & SkuratovskiUi, M. F. (1989). Timalin v kompleksnom lechenii bol’nykh khronicheskim limfoleĭkozom [Thymalin in the combined treatment of patients with chronic lympholeukemia]. Vrachebnoe delo, (3), 47–49.
5. Bach, J., Bardenne, M., Pleau, J., & Rosa, J. (1977). Biochemical characterisation of a serum thymic factor. Nature, 266(5597), 55–57. doi:10.1038/266055a0.
6. Zhaboiedov, H. D., Bychkova, N. H., Skrypnik, R. L., & Sydorova, M. V. (2001). Doslidzhennia stanu klitynnoho i humoral’noho imunitetu ta vyznachennia indyvidual’noï chutlyvosti T-limfotsytiv do imunokorektoriv u khvorykh s diabetychnoiu retynopatiieiu [Evaluation of cellular and humoral immunity and individual sensitivity of T-lymphocytes to immunocorrectors in patients with diabetic retinopathy]. Likars’ka sprava, (1), 53–56.
7. Isaeva, M. P., Budazhabon, G. B., & Kuznik, B. I. (1989). Vliianie timalina na pokazateli immuniteta i gemostaza u bol’nykh rasprostranennymi formami psoziaza [The effect of thymalin on indices of immunity and hemostasis in patients with disseminated forms of psoriasis]. Vestnik dermatologii i venerologii, (10), 42–43.
8. Budazhabon, G. V., Kuznik, B. I., Morozov, V. G., Orlova, N. N., & Khavinson, V. K.h (1984). Sostoianie immunogeneza i gemostaza u bol’nykh s obostreniem khronicheskogo glomerulonefrita, lechennykh timalinom [Immunogenesis and hemostasis in patients with exacerbated chronic glomerulonephritis treated with thymalin]. Terapevticheskii arkhiv, 56(10), 62–66.
9. Maslennikov, A. A., Kamenev, V. F., & Kolomiets, V. M. (2007). Problemy tuberkuleza i boleznei legkikh, (9), 30–33.