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IGF-1 LR3 Peptides and Tissue Growth

IGF-1 LR3 Peptides and Tissue Growth

by | Dec 21, 2022 | Research

 
Scientists have created IGF-1 LR3 peptides by modifying the amino acid sequence of IGF-1. The new peptide has similar potential but possibly higher potency and improved stability. The LR3 in the name describes the two modifications to the IGF-1 molecule. Long R3 IGF-1, or IGF-1 LR3, is an analog of insulin-like growth factor 1 (IGF-1). IGF-1 is an anabolic peptide hormone naturally produced. Primarily, it is considered a mediator of the anabolic effects of growth hormone (HGH). Growth hormone appears to stimulate the production of IGF-1. The IGF-1 produced in the liver is released in the bloodstream and exerts anabolic effects, while the IGF-1 produced in all other tissues acts locally to stimulate growth. The first is R3 which describes the replacement of the 3rd amino acid in IGF-1 with arginine. Scientists ascribed an additional 13 amino acids to the N-terminus of the R3 IGF-1 molecule, turning it into Long R3 IGF-1. IGF-1 LR3 is an experimental peptide with potential anabolic and mitogenic effects.

 

IGF-1 LR3

Scientists developed IGF-1 analogs such as IGF-1 LR3 primarily for experiments to stimulate cell growth. IGF-1 and its analogs appear to be highly anabolic towards actively proliferating cells. They may speed up cell replication, ultimately shortening the time required to create a cell culture and use it to conduct laboratory studies.

IGF-1 LR3 works by activating IGF-1 receptors in most animal cells. Activating these anabolic receptors increases protein synthesis and tissue growth.  IGF-1 LR3 peptide appears to bind to a much lesser degree to IGF-1 proteins than other available analogs. Therefore, its affinity to the anabolic IGF-1 receptors may be much higher, and animal studies show that continuous exposure to IGF-1 LR3 leads to a 2-fold higher anabolic effect than IGF-1. Researchers also noted that “LR3 IGF-I remained more potent than IGF-I in several of these effects even when the peptides were given.“[1]

The reduced affinity to IGF-1 binding proteins may also result in a shorter half-life of IGF-1 LR3 peptide. Animal suggest show that IGF-1 LR3 is eliminated within 4 hours.[2] At the same time, it may induce higher weight gain and organ mass increase in the tested animals compared to IGF-1.

The metabolites of IGF-1 LR3 may have a longer half-life and might remain detectable in test animals for up to 16 hours. In comparison, a high percentage of the natural IGF-1 appears to bind to IGF-1 binding proteins, which may reduce its effectiveness and prolongs half-life by up to 15 hours.[3]

According to one study in a mice model of muscular dystrophy, IGF-1 LR3peptide exposure appeared highly effective in reducing contraction-mediated injury.[4] Contraction damage is a major contributing factor to the pathophysiology of muscular dystrophy.

Another animal trial by Hill et al. also suggested that an IGF-1 LR3 exposure for 8 hours may have a protective effect against loss of muscle mass loss and muscle catabolism during periods of restricted energy intake and caloric deficit. The researchers reported that “Long(R3)-IGF-1 [exposure] tended to preserve whole-body and muscle protein in beef heifers on a low-quality diet.” The continuous exposure also led to significant suppression of the natural IGF-1 synthesis.[5]

One trial in guinea pigs also reported a significant increase in the organ weight of the animals after a 7-day exposure of IGF-1 LR3. The researchers note that the exposure most significantly enlarged the adrenals, gut, kidneys, and spleen.[6] It is important to note that IGF-1 LR3 and all other IGF-1 analogs are only hypothesized to mediate the anabolic effects of growth hormone.

 

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

  1. Tomas FM, Lemmey AB, Read LC, Ballard FJ. Superior potency of infused IGF-I analogues which bind poorly to IGF-binding proteins is maintained when administered by injection. J Endocrinol. 1996 Jul;150(1):77-84. DOI: 10.1677/joe.0.1500077. PMID: 8708565.
  2. Mongongu C, Coudoré F, Domergue V, Ericsson M, Buisson C, Marchand A. Detection of LongR3 -IGF-I, Des(1-3)-IGF-I, and R3 -IGF-I using immunopurification and high resolution mass spectrometry for antidoping purposes. Drug Test Anal. 2021 Jul;13(7):1256-1269. DOI: 10.1002/dta.3016. Epub 2021 Feb 22. PMID: 33587816.
  3. Guler HP, Zapf J, Schmid C, Froesch ER. Insulin-like growth factors I and II in healthy man. Estimations of half-lives and production rates. Acta Endocrinol (Copenh). 1989 Dec;121(6):753-8. doi: 10.1530/acta.0.1210753. PMID: 2558477.
  4. Gehrig SM, Ryall JG, Schertzer JD, Lynch GS. Insulin-like growth factor-I analogue protects muscles of dystrophic MDX mice from contraction-mediated damage. Exp Physiol. 2008 Nov;93(11):1190-8. Doi: 10.1113/expphysiol.2008.042838. Epub 2008 Jun 20. PMID: 18567600.
  5. Hill RA, Hunter RA, Lindsay DB, Owens PC. Action of long(R3)-insulin-like growth factor-1 on protein metabolism in beef heifers. Domest Anim Endocrinol. 1999 May;16(4):219-29. doi: 10.1016/s0739-7240(99)00015-6. PMID: 10370861.
  6. Conlon MA, Tomas FM, Owens PC, Wallace JC, Howarth GS, Ballard FJ. Long R3 insulin-like growth factor-I (IGF-I) infusion stimulates organ growth but reduces plasma IGF-I, IGF-II and IGF binding protein concentrations in the guinea pig. J Endocrinol. 1995 Aug;146(2):247-53. DOI: 10.1677/joe.0.1460247. PMID: 7561636.
  7. Kovacs GT, Worgall S, Schwalbach P, Steichele T, Mehls O, Rosivall L. Hypoglycemic effects of insulin-like growth factor-1 in experimental uremia: can concomitant growth hormone administration prevent this effect? Horm Res. 1999;51(4):193-200. doi: 10.1159/000023357. PMID: 10474022.
  8. MacDonald RS. The role of insulin-like growth factors in small intestinal cell growth and development. Horm Metab Res. 1999 Feb-Mar;31(2-3):103-13. DOI: 10.1055/s-2007-978706. PMID: 10226789.
  9. Dunaiski V, Dunshea FR, Walton PE, Goddard C. Long [R3] insulin-like growth factor-I reduces growth, plasma growth hormone, IGF binding protein-3 and endogenous IGF-I concentrations in pigs. J Endocrinol. 1997 Dec;155(3):559-65. DOI: 10.1677/joe.0.1550559. PMID: 9488001.
  10. Martha S, Pantam N, Thungathurthi S, Rao VL, Devarakonda K. Study of insulin resistance in relation to serum IGF-I levels in subjects with different degrees of glucose tolerance. Int J Diabetes Dev Ctries. 2008 Apr;28(2):54-9. DOI: 10.4103/0973-3930.43100. PMID: 19902049; PMCID: PMC2772007.
Adipotide (FTPP) and Fat Cells

Adipotide (FTPP) and Fat Cells

by | Dec 15, 2022 | Research

Adipotide peptide is a synthetic peptidomimetic and an experimental proapoptotic compound known as FTPP (Fat-Targeted Proapoptotic Peptide). Peptidomimetics are synthetic molecules that may mimic a natural protein’s structural domain. Adipotide appears to bind to the protein receptor prohibitin, which is why it also bears the name Prohibitin-targeting peptide 1 (Prohibitin-TP01). By doing so, it has proapoptotic potential on adipose tissue, meaning that it may induce cell death in white fat cells. Animal studies suggest that by inducing targeted apoptosis, Adipotide peptide may induce fat loss and improvement in several metabolic parameters.

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Adipotide Peptide Overview

Adipotide FTPP appears to act by binding to the receptors for 2 specific proteins, ANXA2 (annexin A2) and prohibitin. Either of these receptors is expressed in various cells, but immunohistochemical analysis suggests that they form specific ANXA2-prohibitin receptor systems in white fat tissue.[1]

Research suggests that these receptors may play a role in regulating fatty acid transport in white adipose tissues.[2] Inhibiting the ANXA2 protein may lead to hypertrophy of white adipose cells due to reduced uptake of fatty acids.

On the other hand, prohibitin is a multifunctional membrane-associated protein that is thought to regulate cell survival and growth. It may trigger apoptosis by shuttling from the cell’s membrane to its nucleus.

Adipotide peptide has a unique structure consisting of the amino-acid sequence GKGGRAKDC-GG-D(KLAKLAK)2. The 9 amino acid sequence CKGGRAKDC appears to bear a specific affinity to the ANXA2-prohibitin receptor system found in the blood vessels supporting white adipose cells.[3] At the same time, (KLAKLAK)2 may disrupt mitochondrial membranes upon receptor-mediated cell internalization and induce programmed cell death.

As Adipotide peptide appears to bind to prohibitin in white adipose vasculature, it may trigger apoptosis and can result in the ablation of white fat cells.

According to research, Adipotide peptide and other similar peptidomimetics may potentially reduce subcutaneous and visceral fat and even target intra-organ fat, such as in fatty liver diseases.[4]

 

Research on Adipotide Peptide

Adipotide peptide may hold potential for two major research focuses –  obesity and cancer. Regarding its metabolic potential and the potential to induce fat loss, the peptidomimetic has been tested in mice, rats, and rhesus monkeys. In obese rats, 28 days of Adipotide peptide exposure led to a 30% reduction in body weight.[5] It also appeared to significantly suppress their appetite, even though the leptin levels of the animals plummeted. Furthermore, the energy expenditure of the animals was not apparently affected.

In another study, the researchers suggested that Adipotide peptide may have led to metabolic improvements as soon as the 3rd day of the study, even before there was a noticeable reduction in the body weight of the tested mice. Kim et al. concluded that Adipotide “rapidly and potently improved the glucose tolerance of obese mice in a weight- and food intake-independent manner.”[6] The peptidomimetic appeared to have reduced triglyceride and insulin levels as well.

In obese rhesus monkeys, Adipotide peptide exposure may have caused white adipose tissue blood vessels to undergo targeted apoptosis.[7] As a result, the tested animals lost weight and improved their insulin sensitivity within the first month of study. A significant decrease in white adipose tissue was noted by dual-energy x-ray absorptiometry and magnetic resonance imaging.

 

Adipotide Peptide and Prostate Cancer

The destruction of white fat may also have positive consequences for prostate cancer. This is suggested to be so, due to a high level of white fat that has been implicated as a critical contributing factor in poor prostate cancer outcomes.[8]

Studied have attempted to examine the impact of Adipotide peptide exposure in research models of prostate cancer. The study evaluated the action of a single cycle of Adipotide peptide in research models of castrate-resistant prostate cancer. According to the study, the models were put through the entire study cycle, but the study was terminated before completion.[9, 10]

 

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

  1. Staquicini FI, Cardó-Vila M, Kolonin MG, Trepel M, Edwards JK, Nunes DN, Sergeeva A, Efstathiou E, Sun J, Almeida NF, Tu SM, Botz GH, Wallace MJ, O’Connell DJ, Krajewski S, Gershenwald JE, Molldrem JJ, Flamm AL, Koivunen E, Pentz RD, Dias-Neto E, Setubal JC, Cahill DJ, Troncoso P, Do KA, Logothetis CJ, Sidman RL, Pasqualini R, Arap W. Vascular ligand-receptor mapping by direct combinatorial selection in cancer patients. Proc Natl Acad Sci U S A. 2011 Nov 15;108(46):18637-42. doi: 10.1073/pnas.1114503108. Epub 2011 Nov 2. PMID: 22049339; PMCID: PMC3219136.
  2. Salameh A, Daquinag AC, Staquicini DI, An Z, Hajjar KA, Pasqualini R, Arap W, Kolonin MG. Prohibitin/annexin 2 interaction regulates fatty acid transport in adipose tissue. JCI Insight. 2016 Jul 7;1(10):e86351. doi: 10.1172/jci.insight.86351. PMID: 27468426; PMCID: PMC4959783.
  3. Kolonin MG, Saha PK, Chan L, Pasqualini R, Arap W. Reversal of obesity by targeted ablation of adipose tissue. Nat Med. 2004 Jun;10(6):625-32. doi: 10.1038/nm1048. Epub 2004 May 9. PMID: 15133506.
  4. Hossen N, Kajimoto K, Akita H, Hyodo M, Harashima H. A comparative study between nanoparticle-targeted therapeutics and bioconjugates as obesity medication. J Control Release. 2013 Oct 28;171(2):104-12. doi: 10.1016/j.jconrel.2013.07.013. Epub 2013 Jul 18. PMID: 23871959.
  5. Kim DH, Woods SC, Seeley RJ. Peptide designed to elicit apoptosis in adipose tissue endothelium reduces food intake and body weight. Diabetes. 2010 Apr;59(4):907-15. doi: 10.2337/db09-1141. Epub 2010 Jan 26. PMID: 20103704; PMCID: PMC2844838.
  6. Kim DH, Sartor MA, Bain JR, Sandoval D, Stevens RD, Medvedovic M, Newgard CB, Woods SC, Seeley RJ. Rapid and weight-independent improvement of glucose tolerance induced by a peptide designed to elicit apoptosis in adipose tissue endothelium. Diabetes. 2012 Sep;61(9):2299-310. doi: 10.2337/db11-1579. Epub 2012 Jun 25. PMID: 22733798; PMCID: PMC3425411.
  7. Barnhart KF, Christianson DR, Hanley PW, Driessen WH, Bernacky BJ, Baze WB, Wen S, Tian M, Ma J, Kolonin MG, Saha PK, Do KA, Hulvat JF, Gelovani JG, Chan L, Arap W, Pasqualini R. A peptidomimetic targeting white fat causes weight loss and improved insulin resistance in obese monkeys. Sci Transl Med. 2011 Nov 9;3(108):108ra112. doi: 10.1126/scitranslmed.3002621. PMID: 22072637; PMCID: PMC3666164.
  8. Allott EH, Masko EM, Freedland SJ. Obesity and prostate cancer: weighing the evidence. Eur Urol. 2013 May;63(5):800-9. doi: 10.1016/j.eururo.2012.11.013. Epub 2012 Nov 15. PMID: 23219374; PMCID: PMC3597763.
  9. Smith, T. L., Sidman, R. L., Arap, W., & Pasqualini, R. (2022). Targeting vascular zip codes: from combinatorial selection to drug prototypes. In The Vasculome (pp. 393-401). Academic Press.
  10. ClinicalTrials.gov [Internet]. National Library of Medicine (US). 2010 Dec 17 – . Identifier NCT01262664, A First-in-Man, Phase I Evaluation of A Single Cycle of Prohibitin Targeting Peptide 1 in Patients With Metastatic Prostate Cancer and Obesity; 2019 Jan 4; http://clinicaltrials.gov/ct2/show/NCT01262664
Semaglutide Research in Hormone Signaling

Semaglutide Research in Hormone Signaling

by | Nov 27, 2022 | Research

Semaglutide is a peptide agonist to the glucagon-like peptide-1 (GLP-1) receptors in the pancreas, the brain, and other organs. The hypothetical action of the compound is considered to be similar to GLP-1, a peptide hormone naturally produced in the intestine. It is an incretin, meaning it is considered to stimulate insulin secretion. Semaglutide is also a subject of extensive research, including pancreatic beta cell apoptosis and neuroprotective potential.

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Semaglutide and Blood Sugar Control

Semaglutide has been hypothesized to act by activating the GLP-1 receptors in the pancreatic beta cells, stimulating insulin synthesis and release.[1][2] The stimulating effect on insulin synthesis is the primary mechanism via which Semaglutide may possibly lower both fasting and postprandial glucose levels. A meta-analysis of 26 RCTs suggests that Semaglutide may lower the fasting blood sugar levels and markers for long-term glucose control, such as HbA1c, in cases of type 2 diabetes.[3]

In addition to stimulating insulin secretion, Semaglutide may potentially reduce glucagon release and suppress hepatic gluconeogenesis.[4] These potential actions are supported by study findings in non-diabetic models, which lasted up to 12 weeks and reported over 38% reduction in blood sugar levels compared to a placebo after a carbohydrate-rich food delivery.[5] The researchers also suggested that Semaglutide may have slowed the speed of gastric emptying during the first hour after caloric intake compared to a placebo. The scientists suggested that this potential of Semaglutide may contribute to a gradual release of glucose and better glycemic control. Yet, the overall speed of gastric emptying over the entire 5-hour monitoring period after the meal appeared not affected.

Semaglutide has been hypothesized to reduce hyperglycemia without causing hypoglycemia. The risk of hypoglycemia is not considered to be higher when compared to a placebo as Semaglutide may possibly stimulate insulin secretion in a glucose-dependent manner.[6] In addition, the inhibition of glucagon release may not occur under hypoglycemic conditions.

 

Semaglutide and Weight

Semaglutide has been suggested to stimulate insulin secretion without leading to weight gain. Studies suggest that Semaglutide may reduce ad libitum energy intake, which may result in weight loss in the long term.[8] According to one study, Semaglutide reduced hunger hormone signaling to the brain, resulting in a reported 24% reduction in energy intake. Semaglutide may activate the GLP-1 receptors in the brain, which may play a major role in modulating appetite and reward-related behavior.[9] Furthermore, the potential of Semaglutide to slow down gastric emptying within the first hour of having a meal may also contribute to a reduced ad libitum energy intake.

 

Pancreatic Beta Cell Survival

Preliminary studies conducted in test animals suggest that Semaglutide may stimulate pancreatic beta cells’ survival and proliferation. These potential actions are considered to be of significant interest since cases of type 2 diabetes are often associated with pancreatic beta cell dysfunction and apoptosis in the long term.[10]

Animal research suggests that Semaglutide may help reverse the harmful changes of obesity and insulin resistance on pancreatic beta cells and stimulate their proliferation.[11] Researchers reveal that some studies also report that GLP-1 antagonists, such as Semaglutide, may protect pancreatic beta cells from apoptosis.[12] Several possible mechanisms are suggested in the protective potential of Semaglutide, and one of the most prominent is reducing the overload on the endoplasmic reticulum of the beta cells in diabetic conditions. GLP-1 receptor activation may also help stimulate autophagy, which prevents beta cell injury and death by protecting against inflammation and oxidative stress.

 

Semaglutide and Neuroprotection

Interestingly, Parkinson’s disease and type 2 diabetes are considered to share several genetic susceptibilities, such as single nucleotide polymorphisms in the growth factor signaling kinase gene Akt.[13] This has sparked interest in researching the potential of diabetes compounds for research studies on Parkinson’s disease. Currently, other GLP-1 receptor agonists, such as Exendin-4, have already been suggested to exhibit protective effects on Parkinson’s cases.[14] Another GLP-1 antagonist, Liraglutide, is under investigation for this hypothetical action.[16]

The research regarding the potential neuroprotective action of Semaglutide is still in its infancy, but many laboratory studies in animal models of PD suggest promising results.[15] The experiments report that Semaglutide may have neuroprotective characteristics and may increasethe survival of the dopaminergic neurons, the apoptosis of which is associated with the development of Parkinson’s.

In animals, Semaglutide appeared to have alleviated the chronic inflammatory responses in the brain, reduced lipid peroxidation, and increased the expression of growth factors that protect dopaminergic neurons in the substantia nigra and striatum.

 

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:

  1. Dhillon S. Semaglutide: First Global Approval. Drugs. 2018 Feb;78(2):275-284. DOI: 10.1007/s40265-018-0871-0. PMID: 29363040.
  2. Hou Y, Ernst SA, Heidenreich K, Williams JA. Glucagon-like peptide-1 receptor is present in pancreatic acinar cells and regulates amylase secretion through cAMP. Am J Physiol Gastrointest Liver Physiol. 2016 Jan 1;310(1):G26-33. doi: 10.1152/ajpgi.00293.2015. Epub 2015 Nov 5. PMID: 26542397; PMCID: PMC4698438.
  3. Zaazouee MS, Hamdallah A, Helmy SK, Hasabo EA, Sayed AK, Gbreel MI, Elmegeed AA, Aladwan H, Elshanbary AA, Abdel-Aziz W, Elshahawy IM, Rabie S, Elkady S, Ali AS, Ragab KM, Nourelden AZ. Semaglutide for the treatment of type 2 Diabetes Mellitus: A systematic review and network meta-analysis of safety and efficacy outcomes. Diabetes Metab Syndr. 2022 Jun;16(6):102511. DOI: 10.1016/j.dsx.2022.102511. Epub 2022 May 20. PMID: 35623229.
  4. Mahapatra MK, Karuppasamy M, Sahoo BM. Semaglutide, a glucagon like peptide-1 receptor agonist with cardiovascular benefits for management of type 2 diabetes. Rev Endocr Metab Disord. 2022 Jun;23(3):521-539. DOI: 10.1007/s11154-021-09699-1. Epub 2022 Jan 7. PMID: 34993760; PMCID: PMC8736331.
  5. Hjerpsted JB, Flint A, Brooks A, Axelsen MB, Kvist T, Blundell J. Semaglutide improves postprandial glucose and lipid metabolism, and delays first-hour gastric emptying in subjects with obesity. Diabetes Obes Metab. 2018 Mar;20(3):610-619. DOI: 10.1111/dom.13120. Epub 2017 Oct 27. PMID: 28941314; PMCID: PMC5836914.
  6. Smits MM, Van Raalte DH. Safety of Semaglutide. Front Endocrinol (Lausanne). 2021 Jul 7;12:645563. doi: 10.3389/fendo.2021.645563. Erratum in: Front Endocrinol (Lausanne). 2021 Nov 10;12:786732. PMID: 34305810; PMCID: PMC8294388.
  7. Mares AC, Chatterjee S, Mukherjee D. Semaglutide for weight loss and cardiometabolic risk reduction in overweight/obesity. Curr Opin Cardiol. 2022 Jul 1;37(4):350-355. DOI: 10.1097/HCO.0000000000000955. Epub 2022 Feb 16. PMID: 35175229.
  8. Blundell J, Finlayson G, Axelsen M, Flint A, Gibbons C, Kvist T, Hjerpsted JB. Effects of once-weekly Semaglutide on appetite, energy intake, control of eating, food preference and body weight in subjects with obesity. Diabetes Obes Metab. 2017 Sep;19(9):1242-1251. DOI: 10.1111/dom.12932. Epub 2017 May 5. PMID: 28266779; PMCID: PMC5573908.
  9. van Bloemendaal L, IJzerman RG, Ten Kulve JS, Barkhof F, Konrad RJ, Drent ML, Veltman DJ, Diamant M. GLP-1 receptor activation modulates appetite- and reward-related brain areas in humans. Diabetes. 2014 Dec;63(12):4186-96. DOI: 10.2337/db14-0849. Epub 2014 Jul 28. PMID: 25071023.
  10. Tomita T. Apoptosis in pancreatic β-islet cells in Type 2 diabetes. Bosn J Basic Med Sci. 2016 Aug 2;16(3):162-79. DOI: 10.17305/bjbms.2016.919. Epub 2016 May 22. PMID: 27209071; PMCID: PMC4978108.
  11. Marinho TS, Martins FF, Cardoso LEM, Aguila MB, Mandarim-de-Lacerda CA. Pancreatic islet cells disarray, apoptosis, and proliferation in obese mice. The role of Semaglutide treatment. Biochimie. 2022 Feb;193:126-136. doi: 10.1016/j.biochi.2021.10.017. Epub 2021 Nov 4. PMID: 34742857.
  12. Costes S, Bertrand G, Ravier MA. Mechanisms of Beta-Cell Apoptosis in Type 2 Diabetes-Prone Situations and Potential Protection by GLP-1-Based Therapies. Int J Mol Sci. 2021 May 18;22(10):5303. doi: 10.3390/ijms22105303. PMID: 34069914; PMCID: PMC8157542.
  13. Xiromerisiou G, Hadjigeorgiou GM, Papadimitriou A, Katsarogiannis E, Gourbali V, Singleton AB. Association between AKT1 gene and Parkinson’s disease: a protective haplotype. Neurosci Lett. 2008 May 9;436(2):232-4. doi: 10.1016/j.neulet.2008.03.026. Epub 2008 Mar 15. PMID: 18395980; PMCID: PMC8958471.
  14. Athauda D, Maclagan K, Skene SS, Bajwa-Joseph M, Letchford D, Chowdhury K, Hibbert S, Budnik N, Zampedri L, Dickson J, Li Y, Aviles-Olmos I, Warner TT, Limousin P, Lees AJ, Greig NH, Tebbs S, Foltynie T. Exenatide once weekly versus placebo in Parkinson’s disease: a randomised, double-blind, placebo-controlled trial. Lancet. 2017 Oct 7;390(10103):1664-1675. DOI: 10.1016/S0140-6736(17)31585-4. Epub 2017 Aug 3. PMID: 28781108; PMCID: PMC5831666.
  15. Zhang L, Zhang L, Li L, Hölscher C. Semaglutide is Neuroprotective and Reduces α-Synuclein Levels in the Chronic MPTP Mouse Model of Parkinson’s Disease. J Parkinsons Dis. 2019;9(1):157-171. DOI: 10.3233/JPD-181503. PMID: 30741689.
  16. Clinical trial identifier NCT02953665
Research in Wrinkle Reduction and Vialox

Research in Wrinkle Reduction and Vialox

by | Sep 23, 2022 | Research

Vialox peptide (also known as Pentapeptide-3V) has been suggested to exhibit potential in preventing muscle contraction by exhibiting a curare-like effect at the neuromuscular junction, disallowing the nervous system signals from reaching the muscles. Vialox peptide is of interest because of its potential to communicate between muscles and nerves.

Vialox peptide has been suggested to interfere with nerve and muscle signal transmission. Signals are transmitted in normal conditions after nerves release acetylcholine from their axons. Contraction may occur after acetylcholine transportation through the neuromuscular junction and binds to a receptor on the muscle.

Vialox peptide may halt contraction by binding to the AChR.[2] Acetylcholine is prevented from binding due to this action, which may induce less binding and fewer muscle contractions.

At the neuromuscular junction, sodium ion release is constrained due to acetylcholine binding to a muscle receptor. Depolarization occurs, which may cause electrical pulses to develop wrinkling and creasing via the muscle contraction. Vialox may inhibit this process by binding to AChR. Vialox peptide inhibits acetylcholine binding when it binds to AChR.

Vialox peptide has been suggested to only affect peripheral AChRs and may not affect central neuronal receptors. Unlike the other nicotinic acetylcholine receptor antagonists. This process suggests that Vialox only acts on the neuromuscular junction. Vialox peptide may potentially reduce skin texture in research cases by up to 11% and relief by 8%, according to one study. Since wrinkle size and ease are considered to be inversely proportional, Vialox may potentially reduce wrinkle development by an average of 8%. Approximately 60% and 47% of the animal subjects were studied.

Vialox (Pentapeptide-3V), composed of lysine, threonine, and serine, is considered to stimulate collagen production while tightening the skin by acting directly on the dermis. Vialox may potentially boost melanin production, a considered protectant against UV 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

  1. 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.
  2. Reddy, B. Y., Jow, T., & Hantash, B. M. (2012). Bioactive oligopeptides in dermatology: Part II. Experimental dermatology, 21(8), 569-575. https://onlinelibrary.wiley.com/doi/10.1111/j.1600-0625.2012.01527.x
Syn-Coll and Collagen Production Stimulation

Syn-Coll and Collagen Production Stimulation

by | Sep 21, 2022 | Research

Syn-coll peptide or Palmitoyl Tripeptide-5 is a peptide that has been hypothesized to increase the production of Type I and Type III collagen while inhibiting its degradation (1). It is also known as Palmitoyl Tripeptide-5 or Tripeptide-5. Syn-coll peptide appears to induce these functions by activating the transforming growth factor.

Research has suggested that Syn-coll may function similarly to Thrombospondin-1 by stimulating the breakdown of collagen caused by transforming growth factors. A naturally occurring peptide called TSP-1 is considered to promote TGF- activity. Syn-coll peptide is suggested to host the same properties as TSP-1 in increasing Type I and III collagen levels in dermal (skin) fibroblasts. According to experimental results, Syn-coll may raise type I and III collagen levels by 2-3 folds above normal levels(2). Varga et al. further suggest, ‘Our results indicate that TGF beta causes a marked enhancement of the production of types I and III collagens and fibronectin by cultured normal … dermal fibroblasts. The rate of collagen production by fibroblasts exposed to TGF beta was 2-3-fold greater than that of control cells. These effects were associated with a 2-3-fold increase in the steady-state amounts of types I and III collagen mRNAs and a 5-8-fold increase in the amounts of fibronectin mRNAs as determined by dot-blot hybridization with specific cloned cDNA probes. In addition, the increased production of collagen and fibronectin and the increased amounts of their corresponding mRNAs remained elevated for at least 72 h after the removal of TGF beta. These findings suggest that TGF beta may play a major role in the normal regulation of extracellular matrix production in vivo and may contribute to the development of pathological states of fibrosis’ (2) TSP-1 is a protein found in the extracellular matrix (ECM), and it is considered to be found alongside collagen and elastin.

Research regarding Palmitoyl Tripeptide-5, like TSP-1, suggests that this peptide may improve wound healing (3). It appears to participate in the development of skin structures. The Syn-coll peptide may inhibits matrix metalloproteinase I and III activity (MMP1 and MMP3). Enzymes that degrade collagen are known as matrix metalloproteinases. These enzymes may be beneficial because they recycle collagen, but appear uncontrollably increased to abnormal levels in conditions such as inflammation. As a result, premature skin damage, lines, and creasing along the skin structure may appear (3).

Syn-coll may potentially support the elimination of toxins and reduce the development and depth of wrinkles on the skin surface. Syn-coll appears to interact with the skin, keeping toxins at bay. This procedure may shield from free radicals.

By possibly inhibiting MMP1 and MMP3 activity, Syn-coll peptide may potentially help to prevent collagen breakdown. These hypotheses suggest that Syn-coll peptide may promote the formation of Type I and Type III collagen while inhibiting collagen breakdown by the enzymes, as mentioned earlier.

Syn-coll, a synthetic peptide component, has been hypothesized to have two primary effects. It appears to increase collagen production by replicating the activation of latent transforming growth factor beta, TGF (Tissue Growth Factor), considered a critical component in collagen synthesis. It appears to protect collagen from breakdown by inhibiting matrix metalloproteinases (MMP). Both activities may work together to keep the skin’s structural integrity intact. Compared to a placebo, Syn-coll peptide may be up to 3.5 times more impactful in wrinkle depth reduction. According to the researchers, Palmitoyl Tripeptide-5 may be 60% more effective than Palmitoyl Pentapeptide (5).

 

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

  1. Errante F, Ledwoń P, Latajka R, Rovero P, Papini AM. Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Front Chem. 2020 Oct 30;8:572923. doi: 10.3389/fchem.2020.572923.
  2. Varga J, Rosenbloom J, Jimenez SA. 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. 1987 Nov 1;247(3):597-604
  3. Resende DISP, Ferreira MS, Sousa-Lobo JM, Sousa E, Almeida IF. Usage of Synthetic Peptides in Cosmetics for Sensitive Skin. Pharmaceuticals (Basel). 2021 Jul 21;14(8):702. doi: 10.3390/ph14080702.
  4. Fadilah NIM, Rahman MBA, Yusof LM, Mustapha NM, Ahmad H. The Therapeutic Effect and In Vivo Assessment of Palmitoyl-GDPH on the Wound Healing Process. Pharmaceutics. 2021 Feb 1;13(2):193. doi: 10.3390/pharmaceutics13020193.
  5. Bucay VW, Day D. Adjunctive skin care of the brow and periorbital region. Clin Plast Surg. 2013 Jan;40(1):225-36. doi: 10.1016/j.cps.2012.09.003
  6. Resende DISP, Ferreira MS, Sousa-Lobo JM, Sousa E, Almeida IF. Usage of Synthetic Peptides in Cosmetics for Sensitive Skin. Pharmaceuticals (Basel). 2021 Jul 21;14(8):702. doi: 10.3390/ph14080702
Pal-GHK Peptide and Experimental Research in Wrinkle Depth

Pal-GHK Peptide and Experimental Research in Wrinkle Depth

by | Sep 19, 2022 | Research

Pal-GHK, also known as Palmitoyl Tripeptide-1 or Palmitoyl Oligopeptide, may act to mitigate the development of creasing in the epidermis and may regulate trans-epidermal water loss.[1,2] Pal-GHK is a peptide with a fatty acid end and a peptide end. Pal-GHK peptide is a fibroblast stimulant and a minor component of the elastin protein.

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Buy Pal-GHK (Palmitoyl Tripeptide-1) (200mg)
 

Potential Function of Pal-GHK Peptide

Palmitoyl Tripeptide-1 may induce the production of fibroblasts at a rapid rate to replenish and regenerate any lost elastin. The GHK-end is connected to the Pal-end, the fatty acid (Palmitoyl) end of Pal-GHK acts as an intermediary. This transport complex appears to improve skin cell penetration.

Pal-GHK peptide appears to activate genes that may change and reset cells. This may be accomplished by attaching Palmitoyl to the peptide sequence, GHK, which may make it more effective for DNA repair genes and increases the expression of the 14 genes that modulate antioxidant production. Following the genetic changes, the action of cell aging may be reduced, as are radicals and toxic agents that cause the development of certain diseases.

Pal-GHK is a modified form of the extracellular matrix-derived peptide GHK that may potentially permeate the stratum corneum and attain the epidermal and dermal skin layers.

Pal-GHK (0.5 M) may increaase collagen synthesis in skin fibroblasts. It may reduce collagen degradation in skin samples exposed to UVA light when examined at a concentration of 6 ppm.

Scientists suggest that combined with the zwitterionic surfactant C12 dodecyl dimethylamine oxide they may investigate the composite’s identity into aggregates, ribbons, and nanobelts. Pal-GHK peptide as an internal standard helped quantify pal-KTTKS in anti-wrinkle creams using LC-MS/MS.

Scientists believe Pal-GHK peptide may activate age-related DNA repair and certain genes. According to new research, the peptide may potentially influence follicle regeneration.

 

Pal-GHK Peptide and Wrinkles

Pal-GHK may protect the extracellular matrix from certain cell aging consequences, according to scientific data[4]. Shagen et al report that “In a study … leading to statistically significant reductions in wrinkle length, depth and skin roughness. Another study applied both vehicle and palmitoyl tripeptide-1 to the skin … documenting a small but statistically significant increase in skin thickness (~4%, compared to the vehicle alone)The peptide accomplishes this by increasing the production of elastin and collagen.”

Palmitoyl Tripeptide-1 may replenish the skin’s extracellular matrix, reducing wrinkles, smoother skin, and less uneven skin. At the same time, it may protect collagen from degradation caused by Ultraviolet A (UVA) rays. Pal-GHK peptide may be examined solely or combinatorally with Palmitoyl tetrapeptide – Z.

 

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

  1. Ferreira, M. S., Magalhães, M. C., Sousa-Lobo, J. M., & Almeida, I. F. (2020). Trending anti-aging peptides. Cosmetics, 7(4), 91.
  2. Gorouhi, F., & Maibach, H. I. (2009). Role of peptides in preventing or treating aged skin. International journal of cosmetic science, 31(5), 327-345.
  3. Park, S. I., An, G. M., Kim, M. G., Heo, S. H., & Shin, M. S. (2020). Enhancement of Skin Permeation of Anti-wrinkle Peptide GHKs Using Cell Penetrating Peptides. Korean Chemical Engineering Research, 58(1), 29-35. https://doi.org/10.9713/KCER.2020.58.1.29