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TB-500 Fragment (17-23) is a research peptide consisting of a short amino acid sequence derived from the actin-binding region of Thymosin Beta-4. It has been shown in preclinical studies to regulate cell migration, angiogenesis, and cytoskeletal organization through modulation of actin polymerization. This fragment is used in experimental research investigating wound repair, tissue remodeling, and peptide-mediated regenerative signaling mechanisms.
TB-500 Fragment (17-23), also called fequesetide or (17) (LKKTETQ) (23), represents the smallest portion of the thymosin beta-4 molecule that retains the larger protein’s active binding domain. Research indicates that this synthetic derivative of thymosin beta-4 is capable of binding to actin, the molecule inside of cells that is responsible for improved cell structure, movement (a.k.a. migration), and replication. By altering the function of actin in cells, TB-500 Fragment (17-23) has been shown to modulate the immune response and alter cell migration patterns. This can lead to large-scale changes in tissue/organ structure and function. In animal models, these changes have been shown to accelerate wound healing, decrease inflammation, promote blood vessel growth, reduce scar formation, improve musculoskeletal function, and help to slow or reverse the course of certain disease conditions.
Biochemical Characteristics
Amino Acid Sequence: LEU-LYS-LYS-THR-GLU-THR-GLN (LKKTETQ)
Chemical Formula: C36H66N10O13
Molecular Weight: 846.97 g/mol
PubChem CID: 10169788
CAS Number: 476014-70-7
Synonyms: Fequesetide; Thymosin Beta-4 (17–23)
The peptide lacks disulfide bonds and exhibits physicochemical properties suitable for aqueous laboratory systems. Structural simplicity enables reproducible synthesis and analytical verification.
Research Applications
Thymosin Beta-4 Fragment (17–23) is employed exclusively in research environments to examine:
- Actin monomer sequestration and filament assembly
- Cellular migration and cytoskeletal remodeling
- Intracellular signal transduction pathways
- Protein–protein interaction dynamics
- Regulation of inflammatory mediators in animal models
All applications are limited to non-clinical experimental models.
Pathway / Mechanistic Context
Mechanistic investigations indicate that the fragment participates in modulation of actin polymerization processes. Interaction with actin-regulatory complexes such as Arp2/3 has been explored in preclinical models, highlighting its utility for studying branched actin network formation.
Downstream signaling pathways associated with cytoskeletal organization, including focal adhesion kinase–related cascades and PI3K/Akt-associated signaling, have been examined in vitro using this peptide as a research tool.
Preclinical Research Summary
Published preclinical literature describes investigation of thymosin beta-4–derived fragments in rodent and cellular systems. Experimental observations include modulation of fibroblast migration, endothelial cell organization, and cytokine signaling under controlled laboratory conditions.
Additional studies in neural and musculoskeletal animal models have explored molecular responses related to cytoskeletal plasticity, inflammatory mediator balance, and cellular differentiation markers. These findings are presented strictly as experimental observations without clinical extrapolation.
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