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 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. In eukaryotic cells, the TB-500 peptide is suggested to bind to actin, inhibit actin polymerization, and may be an actin-cloistering molecule.

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

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


TB-500 Peptide Research

TB-500 peptide may be concentrated at injury sites, where it may improve wound healing and repair in the brain, spinal cord, skin, heart, bones, and organs.[4]

When released from platelets, TB-500 peptide may play a potential cellular role in immune regulation and inflammation. As a result, TB-500 peptide may increase B cells, which regulate antibody activation. It may increase Actin levels to promote tissue repair after injury and potentially stimulate T cell synthesis to improve immune system function.[5]

TB-500 and Blood Clots: TB-500 peptide may be a vital ancillary in mitigating blood clots and might regulate the formation of blood vessels.

TB-500 and Soft Tissue Damage: The potential of TB-500 peptide to promote angiogenesis and reduce inflammation may result in muscle, ligament, and tendon recovery.

TB-500 and Muscular Function: TB-500 peptide may potentially increase the rate of muscle repair and growth rate, including regulating muscle spasms.

TB-500 and Neurological and Cardiovascular Damage: TB-500 peptide may potentially promote angiogenesis, including neuron formation and better brain axonal density.

TB-500 and Matrix Metalloproteinase Expression in Tissue Repair: Wound healing impairment is common in diabetic cases of immobility. According to research, TB-500 peptide may potentially improve 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 normal rats and mice, the peptide appears to potentially promote 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 suggested 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 suggested that the peptide increased MMP-1 and MMP-9 levels.


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  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 peptide, 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.

Dr. Usman

Dr. Usman (BSc, MBBS, MaRCP) completed his studies in medicine at the Royal College of Physicians, London. He is an avid researcher with more than 30 publications in internationally recognized peer-reviewed journals. Dr. Usman has worked as a researcher and a medical consultant for reputable pharmaceutical companies such as Johnson & Johnson and Sanofi.