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PTD-DBM is a synthetic fusion peptide comprising a protein transduction domain and a Dishevelled-binding motif that is studied for its ability to modulate the CXXC5–Dishevelled interaction and Wnt/β-catenin signaling.
A synthetic, cell-penetrating peptide construct called PTD-DBM was created in the lab to study protein–protein interactions between Disheveled (Dvl) and CXXC-type zinc finger protein 5 (CXXC5). Protein transduction domain–Dishevelled-binding motif is abbreviated as PTD-DBM. The peptide's structure consists of an arginine-rich protein transduction domain, a flexible glycine linker, and a Dvl-binding motif derived from CXXC5.
The commonly reported PTD-DBM sequence contains 25 amino-acid residues and has a molecular mass of 3,082.6 g/mol. Its high arginine content imparts a strongly cationic character to the molecule, while the glycine-rich linker provides conformational flexibility between the transduction and binding regions.
PTD-DBM is recognized primarily as an experimental molecular tool for examining the CXXC5–Dvl interaction and associated Wnt/β-catenin signaling processes. Laboratory studies have used biochemical, cellular and structural methods to characterize the interaction between the CXXC5-derived binding motif and the PDZ domain of Dishevelled. The peptide can therefore provide a defined synthetic probe for controlled investigations of intracellular signaling and protein-interaction biology.
PTD-DBM is a linear 25-residue peptide constructed from three functionally distinct sequence regions. The N-terminal segment consists of eight consecutive arginine residues (RRRRRRRR), forming an arginine-rich protein transduction domain. This is followed by a four-residue glycine linker (GGGG) and the C-terminal sequence RKTGHQICKFRKC, which represents the Dishevelled-binding component of the construct.
The abundance of arginine and lysine residues gives PTD-DBM a strongly basic and positively charged molecular character under typical aqueous laboratory conditions. In contrast, the repeated glycine residues introduce relatively little steric restriction and provide flexibility between the two principal regions of the peptide.
Additionally, the C-terminal portion of PTD-DBM has two cysteine residues. Protection from oxidation is important for preserving peptide integrity because thiol-containing cysteine side chains are vulnerable to oxidative alteration under improper handling or storage circumstances.
According to reports, the peptide is easily soluble in water, which is in line with its high percentage of polar and charged residues. The isolated peptide is typically not given a stable globular secondary structure; instead, conformational behavior may change depending on solvent conditions and interactions with molecular binding partners.
Its modular construction distinguishes PTD-DBM from naturally occurring single-domain peptides because the final sequence has been deliberately assembled to combine intracellular transduction and molecular-recognition characteristics.
Current laboratory investigations have examined PTD-DBM primarily as a competitive peptide associated with the interaction between CXXC5 and Dishevelled (Dvl).
CXXC5 has been characterized in experimental literature as a negative-feedback regulator within the canonical Wnt/β-catenin signaling network. Molecular studies indicate that CXXC5 interacts with the PDZ domain of Dishevelled through a defined Dvl-binding motif. Structural research on the Dvl1 PDZ domain has revealed the ligand-binding groove and amino acid residues involved in the recognition of CXXC5-derived peptide sequences.
PTD-DBM incorporates a sequence corresponding to this Dishevelled-binding region together with an arginine-rich protein transduction domain. Published experimental studies describe the synthetic construct as a competitive molecular probe capable of interacting with Dvl and interfering with the formation of the endogenous CXXC5–Dvl complex.
Within experimental cellular systems, disruption of this protein–protein interaction has been examined in relation to downstream components of canonical Wnt signaling. Research has included measurements of β-catenin localization, pathway-associated reporter activity and changes in molecular signaling markers. These observations are used to investigate how CXXC5-mediated negative feedback contributes to regulation of the Wnt pathway rather than to establish a clinical or therapeutic function for PTD-DBM.
The N-terminal polyarginine region forms an additional element of the experimental design. Arginine-rich protein transduction domains are used in molecular research to facilitate cellular entry of attached peptide sequences. In PTD-DBM, this domain enables researchers to investigate the Dvl-binding sequence within intracellular experimental systems.
Consequently, PTD-DBM is principally characterized as a synthetic protein–protein interaction competitor and intracellular signaling research peptide.
This summary reflects findings reported in published preclinical and in vitro research. The original studies supporting this information are listed in the references.
As a molecular rival of the interaction between CXXC5 and Disheveled, PTD-DBM has been investigated. This system is used in experiments to describe binding behavior and look into how particular protein domains contribute to intracellular signaling complexes.
Laboratory models have incorporated PTD-DBM into investigations of canonical Wnt/β-catenin signaling. Experimental measurements have included β-catenin localization, pathway reporter systems and signaling-protein analysis following modification of CXXC5–Dvl interactions.
The Dishevelled PDZ domain has been studied using crystallography, nuclear magnetic resonance and molecular modeling. Research involving CXXC5-derived binding sequences has helped characterize the binding pocket and molecular contacts associated with Dvl recognition.
A model for researching arginine-rich protein transduction domains is provided by the octa-arginine region of PTD-DBM. Peptide sequence, charge, and intracellular transport in regulated biological systems can all be studied in the lab.
PTD-DBM can also be studied through peptide chemistry and biophysical approaches directed at sequence-dependent properties, binding specificity and molecular recognition. These investigations provide information about how a synthetic peptide motif interacts with a defined protein domain.
Experimental cell systems have used PTD-DBM to investigate signaling events associated with modification of the CXXC5–Dvl interaction. Such studies may incorporate immunoblotting, reporter assays, microscopy and molecular-expression analysis to characterize pathway behavior.
PTD-DBM can be produced using solid-phase peptide synthesis (SPPS), in which amino acids are sequentially assembled according to the defined 25-residue sequence. Following synthesis and cleavage from the solid support, purification may be performed using preparative chromatographic techniques to separate the target peptide from truncated sequences and other synthesis-related components.
Reverse-phase high-performance liquid chromatography (RP-HPLC) can be used to evaluate chromatographic purity, but liquid chromatography–mass spectrometry (LC-MS) or comparable mass-spectrometric methods can be used to confirm molecular identity by comparing the observed molecular mass with the theoretical value.
Additional analytical parameters may include peptide content, appearance and assessment of synthesis-related impurities where relevant.
Each commercial batch should be supported by a batch-specific Certificate of Analysis (COA) identifying the compound, lot or batch number, testing date, analytical method and measured purity. The purity stated on the product page should correspond directly with the current COA rather than a generic specification.
No certificate has been published for this compound yet.
PTD-DBM, which is given as a lyophilized peptide, needs to be kept dry and shielded from moisture and unneeded light. Published supplier data typically recommends storage at 2–8°C for long-term laboratory storage; lower temperatures may be utilized for longer store times.
Because the sequence contains cysteine residues, unnecessary exposure to oxidizing conditions should be minimized. Repeated temperature cycling should also be avoided because condensation and repeated freeze/thaw events may contribute to degradation of peptide material.
Use a suitable research-grade solvent or buffer chosen in accordance with the specifications of the experimental procedure when producing PTD-DBM for laboratory analysis. To cut down on the number of freeze/thaw cycles, prepared solutions should be aliquoted whenever possible.
Storage requirements should ultimately follow the conditions specified for the individual batch and analytical documentation.
PTD-DBM is a synthetic 25-amino-acid peptide composed of an arginine-rich protein transduction domain, a glycine linker and a Dishevelled-binding motif. It has been investigated as a molecular research tool for studying CXXC5–Dishevelled interactions and associated signalling processes.
PTD-DBM stands for protein transduction domain–Dishevelled-binding motif. The name describes the two principal functional regions incorporated into the synthetic peptide construct.
The commonly indexed PTD-DBM sequence is: RRRRRRRRGGGGRKTGHQICKFRKC It contains 25 amino-acid residues, including an eight-arginine protein transduction domain and a four-glycine linker.
No, a synthetic fusion peptide is what PTD-DBM is. Although the entire PTD-linker-DBM complex is designed for experimental research, its individual sequence elements are taken from known molecular patterns.
Published laboratory studies have examined PTD-DBM in relation to the interaction between CXXC5 and the PDZ domain of Dishevelled. The peptide has been characterized as a competitive probe for investigating this protein–protein interaction and its relationship with canonical Wnt/β-catenin signaling.
Analytical identification may combine RP-HPLC with mass spectrometry such as LC-MS. HPLC provides information about chromatographic purity, while mass spectrometry can be used to compare the experimentally detected molecular mass with the expected molecular mass of approximately 3,082.6 g/mol.
For research and laboratory use only. Not for human or animal consumption.
PTD-DBM is supplied solely as a research material for qualified laboratory and analytical investigation. Information provided on this page relates only to its chemical identity, molecular properties, analytical characterisation and published experimental research context. It is not intended for diagnosis, treatment, cure or prevention of any disease or condition.
