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Thymosin β4 and TB-500
Thymosin β4 is a small, ubiquitous protein whose main functional domain is G-actin binding: it sequesters actin monomers and regulates cytoskeletal dynamics, essential for cell migration. TB-500 is a synthetic fragment that reproduces the active actin-binding domain. The lines of research are the migration of progenitor cells toward the damaged area, angiogenesis and repair, including cardiac tissue models.
GHK-Cu
GHK-Cu (glycyl-L-histidyl-L-lysine complexed with copper) is a tripeptide with high affinity for the copper(II) ion. Its research interest lies in:
- Extracellular matrix remodeling: modulation of the synthesis of collagen, elastin and glycosaminoglycans, and the balance of metalloproteinases.
- Dermal repair and wound healing signaling.
- Modulation of gene expression: transcriptomic studies describe GHK shifting the expression of a large number of genes toward a regenerative profile.
These peptides do not "build" tissue by themselves: they act as signals that orchestrate cell migration, blood supply and matrix remodeling. Understanding them as signaling modulators —not as building material— is key to interpreting the literature correctly.
Catalogue compounds mentioned in this lesson
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