TB-500 Research in Regards to Blood Vessel Growth and Wound Healing

by | Sep 16, 2022 | Research

TB-500 peptide is a synthetic version of Thymosin Beta-4 found in all human and animal cells[1]. TB-500 is a peptide sequence composed of 43 amino acid molecules and a member of 16 cohabiting molecules with high sequence conservation and localization in tissues and circulating cells throughout the body. In eukaryotic cells, the TB-500 peptide binds to actin, inhibits actin polymerization, and is the actin-cloistering molecule.


According to studies, TB-500 is upregulated four to sixfold after early blood vessel formation[2]. It promotes the formation of new blood vessels from existing ones. Following subcutaneous administration, the peptide stimulates wound healing. It upregulates the rejuvenating time of muscle fibers and their cells. TB-500 peptide also promotes cell migration by interacting with actin in the cell cytoskeleton. The central small amino acid long-actin binding domain is responsible for wound healing and blood cell reproduction. These characteristics are activated by increasing endothelial cell migration and keratinocytes, increasing the synthesis of Extra matrix-degrading enzymes.

According to scientific evidence, TB-500 is a synthetic peptide with wound healing and anti-inflammatory properties[2]. This peptide differs from others in that it promotes keratinocyte and endothelial migration. It has a low molecular weight and does not bind to the extracellular matrix, implying that it can travel long distances through tissues. The most important mechanism of action of the TB-500 is its ability to modulate actin activity.


Potential Benefits and Functions of TB-500 Peptide

  • TB-500 is concentrated at injury sites, where it can improve wound healing and repair in the brain, spinal cord, skin, heart, bones, and organs[4].
  • When released from platelets, TB-500 peptide plays a critical cellular role in immune regulation and inflammation. As a result, TB-500 increases B cells, which regulates antibody activation. It increases Actin levels to promote tissue repair after injury and stimulates T cell synthesis to improve immune system function[5].
  • The Impact of TB-500 on Blood Clots: TB-500 is a vital ancillary in treating blood clots and can regulate the formation of blood vessels.
  • The Functions of TB-500 Peptide in Soft Tissue Damage: The ability of TB-500 to promote angiogenesis and reduce inflammation results in muscle, ligament, and tendon recovery.
  • TB-500 and Muscular Function: TB-500 effectively increases the rate of muscle repair and growth rate, including regulating muscle spasms.
  • How TB-500 Impacts Neurological and Cardiovascular Damage: TB-500 can promote angiogenesis, including neuron formation and better brain axonal density.
  • How TB-500 Encourages Matrix Metalloproteinase Expression in wound repair: Wound healing impairment is common in diabetic patients who are immobilized. According to research, TB-500 peptide improves dermal wound repair in rats, dB/dB diabetic mice, and aged mice[6]. Philip et al. concluded that thymosin β4 is active for wound repair in models of impaired healing and may have efficacy in chronic wounds in humans. In normal rats and mice, the peptide promotes corneal repair. TB-500 may regulate matrix metalloproteinase (MMP) expression in wound repair cells. RT-PCR analysis of whole excised mouse dermal wounds on days 1, 2, and 3 after injury showed that TB-500 peptide increased the expression of several metalloproteinases, including MMP-2 and -9, by several folds on days two after wounding. The metalloproteinases secreted by activated monocytes in response to exogenous TB-500 in the wound were also studied. They discovered that the peptide increased MMP-1 and MMP-9 levels. In conclusion, TB-500 is essential for remodeling the extracellular matrix after wound repair.



TB-500 peptide is a research peptide/chemical limited to educational and clinical purposes, not for human use or consumption.

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.



  1. Ho, E. N., Kwok, W. H., Lau, M. Y., Wong, A. S., Wan, T. S., Lam, K. K., Schiff, P. J., & Stewart, B. D. (2012). Doping control analysis of TB-500, a synthetic version of an active region of thymosin β₄, in equine urine and plasma by liquid chromatography-mass spectrometry. Journal of chromatography. A, 1265, 57–69. https://doi.org/10.1016/j.chroma.2012.09.043
  2. Grant, D. S., Rose, W., Yaen, C., Goldstein, A., Martinez, J., & Kleinman, H. (1999). Thymosin beta4 enhances endothelial cell differentiation and angiogenesis. Angiogenesis, 3(2), 125–135. https://doi.org/10.1023/a:1009041911493
  3. Malinda, K. M., Sidhu, G. S., Mani, H., Banaudha, K., Maheshwari, R. K., Goldstein, A. L., & Kleinman, H. K. (1999). Thymosin beta4 accelerates wound healing. The Journal of investigative dermatology, 113(3), 364–368. https://doi.org/10.1046/j.1523-1747.1999.00708.x
  4. Goldstein, A. L., Hannappel, E., & Kleinman, H. K. (2005). Thymosin β4: actin-sequestering protein moonlights to repair injured tissues. Trends in molecular medicine, 11(9), 421-429.
  5. Huff, T., Otto, A. M., Müller, C. S., Meier, M., & Hannappel, E. (2002). Thymosin β4 is released from human blood platelets and attached by factor XIIIa (transglutaminase) to fibrin and collagen. The FASEB journal, 16(7), 691-696.
  6. Philp, D., Badamchian, M., Scheremeta, B., Nguyen, M., Goldstein, A. L., & Kleinman, H. K. (2003). Thymosin β4 and a synthetic peptide containing its actin‐binding domain promote dermal wound repair in db/db diabetic mice and in aged mice. Wound repair and regeneration, 11(1), 19-24.