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TB-500 is a synthetic peptide corresponding to an actin-binding region of thymosin beta-4, a small, highly polar actin-sequestering protein that is one of the most abundant intracellular proteins in mammalian cells. It belongs to the actin-binding peptide class.
In the published preclinical literature, thymosin beta-4 has been characterised at the molecular level as a regulator of the actin cytoskeleton: it binds monomeric G-actin in a 1:1 complex and shifts the equilibrium between monomeric and filamentous actin. In-vitro and cultured-cell work has mapped how it sits along the actin monomer, how that interaction depends on the bound ATP or ADP nucleotide, and how the N-terminal actin-binding motif governs the stability of the complex. It is supplied as a research compound and is not intended for human or veterinary use.
TB-500 corresponds to an actin-binding region of thymosin beta-4, which has been characterised in preclinical laboratory models. The primary studies below, in cell-free biochemical assays and in cultured cells, examined how the peptide binds the actin monomer, how that binding tracks the bound nucleotide, and how it sets the monomer-to-filament equilibrium. The literature is preclinical; it describes the compound, not any outcome in humans.
In vitro
Thymosin beta-4 binds the actin monomer in an extended conformation, contacting both the barbed-end and pointed-end faces
Using circular dichroism, NMR, and cross-linking, the study placed thymosin beta-4 in an extended conformation along the actin monomer, contacting both the barbed-end and pointed-end faces and forming a 1:1 complex that blocks polymerization and nucleotide exchange.
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In vitro
The N-terminus and central actin-binding motif of thymosin beta-4 govern the stability of its complex with the actin monomer
By substituting and modifying single residues across the N-terminal segment and the central actin-binding motif of thymosin beta-4, the study mapped the residues that set the stability of its 1:1 complex with the actin monomer.
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In vitro
The ATP and ADP nucleotide state of the actin monomer modulates its interaction with thymosin beta-4
In cell-free assays, thymosin beta-4 bound MgATP-actin with roughly fifty-fold higher affinity than MgADP-actin, tying its monomer-sequestering activity to the nucleotide state of the actin monomer as a measured endpoint.
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In vitro
Thymosin beta-4 and profilin act as opposing controllers of actin nucleotide exchange on the monomer
In biochemical assays, bound thymosin beta-4 blocked nucleotide exchange on the actin monomer while profilin promoted it, framing the two as opposing controllers of the monomer pool that set the rate and extent of polymerization.
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Full documentation, on the record. A Certificate of Analysis and a Safety Data Sheet are available on request for every batch.
View the Certificate of Analysis ↗Links open the original study on PubMed. For research and educational purposes, descriptive of the published preclinical literature, not therapeutic claims about any ai-peptides product.
