Hexokinase II VDAC Binding Domain Peptide reproduces the mitochondrial-anchoring segment recognized by VDAC at the outer membrane. Hydrophobic and basic residues arrange to interact with the channel surface. Researchers use it to map binding interfaces, study metabolic coupling, and disrupt protein-protein association in model systems. Applications include mitochondrial biology, interaction mapping, and peptide-competition assays.
CAT No: R2861
Hexokinase II VDAC binding domain peptide is a synthetic peptide that corresponds to the specific amino acid sequence within the N-terminal region of Hexokinase II responsible for its interaction with the voltage-dependent anion channel (VDAC) on the outer mitochondrial membrane. As a research tool, this peptide enables precise interrogation of the protein-protein interface between Hexokinase II and VDAC, a critical interaction implicated in the regulation of mitochondrial metabolism, apoptosis, and cellular energy homeostasis. The ability to selectively mimic or disrupt this binding site provides significant value for studies investigating mitochondrial function, metabolic flux, and the molecular mechanisms underlying cell survival and death.
Protein-protein interaction studies: The Hexokinase II VDAC binding domain peptide is widely used to probe the molecular determinants of the Hexokinase II-VDAC interaction. By introducing this peptide into in vitro binding assays or cell-based systems, researchers can competitively inhibit the endogenous association between Hexokinase II and VDAC, thereby elucidating the structural requirements and regulatory factors that govern this critical protein-protein interface. Such studies are essential for mapping interaction domains, validating mutagenesis results, and understanding the dynamic modulation of mitochondrial association by cellular signaling pathways.
Mitochondrial function analysis: Experimental use of the VDAC binding domain peptide enables targeted disruption of Hexokinase II localization to the mitochondria, which has profound effects on mitochondrial physiology. By displacing endogenous Hexokinase II from the outer mitochondrial membrane, the peptide facilitates direct assessment of changes in mitochondrial membrane potential, ATP production, and susceptibility to permeability transition. These studies are particularly valuable for dissecting the metabolic and bioenergetic consequences of altered enzyme-organelle interactions in various cellular contexts.
Apoptosis research: The peptide's ability to modulate the Hexokinase II-VDAC interaction provides a powerful approach for investigating the mitochondrial pathway of apoptosis. Displacement of Hexokinase II from VDAC has been shown to sensitize cells to apoptotic signals, making the peptide an important tool for examining the mechanisms by which mitochondrial binding of metabolic enzymes influences cytochrome c release, caspase activation, and programmed cell death. Use of the peptide in such studies helps clarify the role of mitochondrial anchoring in cellular survival pathways.
Metabolic pathway studies: By selectively interfering with the mitochondrial association of Hexokinase II, the VDAC binding domain peptide is instrumental in elucidating the broader metabolic consequences of enzyme compartmentalization. Researchers employ the peptide to examine alterations in glycolytic flux, glucose uptake, and the integration of glycolysis with oxidative phosphorylation. These applications are crucial for understanding how spatial regulation of key metabolic enzymes impacts cellular energy balance and metabolic adaptability under physiological and stress conditions.
Peptide-based screening and inhibitor development: The Hexokinase II VDAC binding domain peptide serves as a reference standard or template in the design and screening of novel small molecules or modified peptides intended to modulate the Hexokinase II-VDAC interaction. By providing a defined binding motif, it enables high-throughput assays aimed at identifying compounds that either mimic or disrupt this interaction, supporting the development of research tools for dissecting mitochondrial regulation or for chemical biology applications targeting metabolic control points.
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