Dyrktide

Product Name: Dyrktide

Sequence One Letter Code: RRRFRPASPLRGPPK

Sequence Three Letter Code: H-Arg-Arg-Arg-Phe-Arg-Pro-Ala-Ser-Pro-Leu-Arg-Gly-Pro-Pro-Lys-OH

Chemical Formula:C79H135N31O17

Molecular Weight: 1791.2

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: peptide substrate

Conjugation: Unconjugated

Code Nacres: NA.26

Application: Dyrktide is a synthetic peptide optimized as a phosphorylation substrate for DYRK1A, a dual-specificity kinase that autophosphorylates on tyrosine residues and phosphorylates serine/threonine residues on target proteins. DYRK1A plays critical roles in neuronal development, synaptic plasticity, and brain morphogenesis and has been implicated in Down syndrome, autism spectrum disorders, and neurodegenerative diseases. Dyrktide is widely used in in vitro kinase assays to quantify DYRK1A catalytic activity, assess ATP-dependent phosphorylation kinetics, and evaluate inhibitor potency. The peptide also supports studies of substrate recognition and kinase specificity. It is well suited for biochemical, pharmacological, and signaling investigations related to neurodevelopment and kinase-targeted therapeutic discovery.

Current Research: Protein phosphorylation is a central regulatory mechanism controlling cellular signaling, protein function, and gene expression. Protein kinases catalyze the transfer of phosphate groups from ATP to specific amino acid residues on target proteins, thereby modulating numerous biological processes. One kinase that has attracted significant research interest is DYRK1A (Dual-specificity tyrosine-regulated kinase 1A), a member of the DYRK family that plays important roles in neuronal development and brain function. To facilitate biochemical studies of this enzyme, researchers commonly use Dyrktide, a synthetic peptide specifically optimized as a phosphorylation substrate for DYRK1A. The DYRK1A Kinase and Its Dual-Specificity Activity DYRK1A belongs to the family of dual-specificity protein kinases, meaning it can phosphorylate different types of amino acid residues depending on the context. During its maturation, DYRK1A undergoes autophosphorylation on a tyrosine residue within its activation loop, a step required for full catalytic activation. Once activated, the kinase primarily phosphorylates serine and threonine residues on downstream target proteins. Through these phosphorylation events, DYRK1A regulates numerous cellular processes, including transcriptional control, cell cycle progression, and intracellular signaling. Because kinase activity must be tightly controlled to maintain cellular homeostasis, tools that enable precise measurement of enzyme activity are essential for understanding its biological functions. Biological Functions of DYRK1A DYRK1A is highly expressed in the developing and adult nervous system, where it contributes to neuronal differentiation, dendritic growth, and synaptic function. The kinase influences signaling pathways that regulate neural progenitor proliferation and neuronal maturation, making it a key factor in brain morphogenesis and neural circuit formation. In addition to its developmental roles, DYRK1A also participates in regulating transcription factors and signaling proteins involved in neuronal plasticity. These functions contribute to learning, memory formation, and adaptive responses within neural networks. Because of these diverse roles, dysregulation of DYRK1A activity can significantly affect neurological development and function. DYRK1A in Human Disease Abnormal DYRK1A expression or activity has been linked to several neurological and neurodevelopmental disorders. One of the most well-known associations is with Down syndrome, where the DYRK1A gene is located on chromosome 21. Individuals with trisomy 21 carry an extra copy of this chromosome, leading to increased DYRK1A expression that is thought to contribute to cognitive deficits and developmental abnormalities. DYRK1A has also been implicated in autism spectrum disorders, where altered kinase activity may affect neuronal connectivity and synaptic regulation. In addition, the kinase has been studied in the context of neurodegenerative diseases, where it may influence processes such as tau phosphorylation and neuronal stress responses. These disease associations have made DYRK1A an important target for therapeutic research. Design and Purpose of the Dyrktide Peptide Dyrktide is a synthetic peptide specifically engineered to serve as an efficient substrate for DYRK1A. The peptide contains a sequence motif that is readily recognized and phosphorylated by the kinase, allowing researchers to monitor enzymatic activity in a controlled in vitro environment. Because the peptide sequence is optimized for DYRK1A recognition, it provides a reliable and reproducible readout of kinase activity. This makes it particularly useful in biochemical assays designed to quantify phosphorylation events. Using a defined peptide substrate simplifies experimental analysis compared with studying complex protein substrates that may contain multiple phosphorylation sites. Applications in In Vitro Kinase Assays One of the primary uses of Dyrktide is in in vitro kinase assays. In these experiments, purified DYRK1A is incubated with the peptide substrate and ATP, allowing phosphorylation of the peptide to occur. The extent of phosphorylation can then be measured using various detection methods, such as radiolabeled ATP incorporation, fluorescence-based assays, or mass spectrometry. These assays enable researchers to quantify DYRK1A catalytic activity, determine reaction rates, and analyze enzyme kinetics under different experimental conditions. Because the peptide substrate provides a consistent and well-defined target, it allows precise comparison of enzyme activity across multiple experiments. Studying Kinase Kinetics and ATP Dependence Dyrktide is also valuable for examining ATP-dependent phosphorylation kinetics. By varying concentrations of ATP or the peptide substrate, researchers can determine kinetic parameters such as catalytic efficiency and substrate affinity. These kinetic analyses provide insight into how DYRK1A interacts with substrates and how different factors influence its enzymatic activity. Understanding these kinetic properties is important for clarifying how DYRK1A functions within cellular signaling networks. Evaluating DYRK1A Inhibitors Because DYRK1A is implicated in several neurological disorders, there is considerable interest in developing small-molecule inhibitors that modulate its activity. Dyrktide-based kinase assays provide a convenient platform for evaluating candidate compounds. In inhibitor screening experiments, the ability of a compound to reduce phosphorylation of the Dyrktide substrate is measured. This allows researchers to assess inhibitor potency, specificity, and mechanism of action. Such assays are widely used in early-stage drug discovery programs targeting kinase signaling pathways. Investigating Substrate Recognition and Kinase Specificity Beyond measuring enzyme activity, Dyrktide can also be used to study substrate recognition and specificity. By comparing phosphorylation of modified peptide variants or alternative substrates, researchers can determine which sequence features are most important for DYRK1A recognition. These studies help define the structural determinants that guide kinase–substrate interactions and contribute to understanding how DYRK1A selects its physiological targets. Conclusion Dyrktide is a synthetic peptide substrate specifically optimized for phosphorylation by DYRK1A, a dual-specificity kinase involved in neuronal development and signaling. By providing a reliable and well-defined substrate, the peptide enables precise measurement of kinase activity in biochemical assays. Its applications include in vitro kinase activity assays, kinetic analysis of ATP-dependent phosphorylation, evaluation of kinase inhibitors, and studies of substrate recognition mechanisms. Through these experimental uses, Dyrktide supports research into the biological functions of DYRK1A and the development of therapeutic strategies targeting kinase signaling in neurodevelopmental and neurodegenerative diseases.