Amino acid L-Cysteine chemical structure

L-Cysteine Fight Free Radicals

  • Produce Glutathione
  • Build antioxidants
  • Support cellular respiration
  • Detoxification | Anti inflammatory agent
  • Support Keratin & Collagen

Conditionally essential (during times of stress) Organic amino acid

L-Cysteine is one of only two amino acids containing sulfur found in proteins. A conditionally essential amino acid, L-Cysteine tends to be less abundant in humans, yet vastly important to the body. It serves as a precursor for the tripeptide Glutathione, a powerful Antioxidant. Glutathione fights electrophiles and oxidants. L-Cysteine is also responsible for aiding Metal binding, which stabilizes proteins and cellular structures.

L-Cysteine is a powerful Antioxidant against Reactive Oxygen Species (ROS). ROS is a dangerous free radical by-product of Mitochondrion ATP (Adenosine Triphosphate) production. ROS damages cellular DNA and RNA. An increase of ROS production is part of Mitochondrion weakening, and the consequent oxidative stress of mitochondrion weakening accelerates aging.
Fighting ROS production and mitochondria decay is extremely important to healthy aging. On the outside L-Cysteine also slows aging by helping stimulate hair growth and naturally vibrant skin. While internally L-Cysteine is necessary for Mycothiol production an initial detoxification agent against Reactive Oxygen Species (ROS) molecules. Mycothiol is a Thiol compound that is one of the first molecules to battle oxidative stressors.

L-Cysteine also serves many anti inflammatory purposes, helping inhibit endothelial inflammation, and study shows that “appropriate dietary supplement” with L-Cysteine as one of the ingredients may fight Atherosclerosis and vasculitius in humans. Show moreHide Text...

Sources

  • Hasegawa, S., Ichiyama, T., Sonaka, I., Ohsaki, A., Okada, S., Wakiguchi, H., … Furukawa, S. (2012). Cysteine, histidine and glycine exhibit anti-inflammatory effects in human coronary arterial endothelial cells. Clinical and Experimental Immunology, 167(2), 269–274.
  • Lu, C.-H., Lin, Y.-F., Lin, J.-J., & Yu, C.-S. (2012). Prediction of Metal Ion–Binding Sites in Proteins Using the Fragment Transformation Method. PLoS ONE, 7(6), e39252. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3377655/
  • Marí, M., Morales, A., Colell, A., García-Ruiz, C., & Fernández-Checa, J. C. (2009). Mitochondrial Glutathione, a Key Survival Antioxidant. Antioxidants & Redox Signaling, 11(11), 2685–2700. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2821140/
  • National Center for Biotechnology Information. PubChem Compound Database; CID=5862, https://pubchem.ncbi.nlm.nih.gov/compound/5862 (accessed Sept. 18, 2017).
  • Newton, G. L., Buchmeier, N., & Fahey, R. C. (2008). Biosynthesis and Functions of Mycothiol, the Unique Protective Thiol of Actinobacteria. Microbiology and Molecular Biology Reviews: MMBR, 72(3), 471–494.
  • Poole, L. B. (2015). The Basics of Thiols and Cysteines in Redox Biology and Chemistry. Free Radical Biology & Medicine, 0, 148–157.
  • Steiner, E. , Böth, D. , Lössl, P. , Vilaplana, F. , Schnell, R. , et al. (2014). Cysk2 from mycobacterium tuberculosis is an o-phospho-l-serine-dependent s-sulfocysteine synthase. Journal of Bacteriology, 196(19), 3410. http://jb.asm.org/content/196/19/3410.full