Description
PTD‑DBM Peptide
PTD‑DBM is a synthetic cell‑penetrating peptide linked to a Dishevelled Binding Motif (DBM). As a cell‑penetrating peptide (CPP), PTD‑DBM has been developed to assist the delivery of biologically active sequences into cells by enhancing membrane translocation. The DBM portion of the peptide is derived from a consensus region that binds to the Dishevelled (Dvl) protein, a critical component of cellular signaling pathways including Wnt signaling. The combination of PTD (peptide transduction domain) and DBM is often studied for its potential to modulate intracellular signaling pathways by enabling transport of inhibitory sequences into cells.
Chemical Makeup
Molecular Formula: C₄₁H₆₇N₁₃O₉
Molecular Weight: 813.0 g/mol
Other Known Titles: PTD‑DBM peptide, peptide transduction domain dishevelled binding motif
Research and Experimental Data
PTD‑DBM and Cell Signaling
Researchers have examined the use of PTD‑DBM constructs to influence Wnt/β‑catenin signaling, a pathway involved in cell growth, differentiation, and development. In some in‑vitro models, cell‑penetrating peptides linked to the dishevelled binding motif have been shown to interrupt protein‑protein interactions, potentially providing tools for probing the effects of Wnt signaling modulation.
PTD‑DBM and Cellular Uptake
CPPs like PTD have been studied for their ability to carry attached peptide sequences across cell membranes more efficiently than the sequences alone. In research settings, PTD‑tagged motifs may help support intracellular delivery of ligands, inhibitory peptides, or cargo sequences that otherwise would not easily enter cells.
PTD‑DBM and Target Pathways
Work in cell cultures suggests that PTD‑DBM may assist in studies aimed at regulating intracellular signaling associated with cell migration, stem cell differentiation, and pathway modulation in models of tissue growth and repair.
PTD‑DBM peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering.
