P110 is a peptide designed to modulate dynamin-related protein interactions by mimicking specific recognition motifs. Hydrophobic and charged residues contribute to folding and target-binding fidelity. Researchers assess its conformational preferences and binding thermodynamics. Applications include mitochondrial-dynamics studies, motif-function characterization, and PPI-inhibition modeling.
CAT No: R2808
P110 is a synthetic peptide compound specifically designed to modulate mitochondrial dynamics by selectively inhibiting the interaction between the mitochondrial fission protein Drp1 and its receptor Fis1. As a research-use peptide, P110 has gained significant attention in the field of mitochondrial biology due to its ability to selectively block pathological mitochondrial fission without disrupting physiological mitochondrial division. This targeted mechanism makes P110 a valuable molecular tool for investigating the role of mitochondrial fragmentation in a variety of cellular processes, particularly those associated with oxidative stress, neurodegeneration, and apoptosis. Its unique specificity and functional significance have positioned it as a critical reagent for dissecting the molecular pathways underlying mitochondrial dysfunction in diverse experimental systems.
Mitochondrial Dynamics Research: P110 is widely utilized in studies aimed at elucidating the molecular mechanisms governing mitochondrial fission and fusion. By specifically inhibiting Drp1-Fis1 interaction, the peptide enables researchers to dissect the contribution of excessive mitochondrial fragmentation to cellular pathologies. Its use allows for precise modulation of mitochondrial morphology, providing insights into the balance between fission and fusion events and their impact on cellular homeostasis. This is particularly valuable in experimental models where mitochondrial dynamics are implicated in disease progression or cellular stress responses.
Neurodegeneration Models: The compound has become an essential tool in the investigation of neurodegenerative diseases, where aberrant mitochondrial fragmentation is a hallmark feature. By applying P110 in neuronal cell cultures or animal models, researchers can assess the impact of targeted fission inhibition on neuronal survival, synaptic function, and the progression of neurodegenerative phenotypes. The peptide's specificity for the pathological, but not physiological, mitochondrial fission pathway enables the study of mitochondrial contributions to neurotoxicity and neuronal loss without interfering with essential cellular functions.
Oxidative Stress and Apoptosis Studies: P110 is instrumental in research focused on the interplay between mitochondrial dynamics, reactive oxygen species (ROS) production, and apoptosis. By preventing excessive mitochondrial fission, the peptide aids in evaluating how mitochondrial morphology influences ROS generation and the activation of apoptotic pathways. This application is particularly relevant in models of cellular injury, ischemia-reperfusion, or toxin exposure, where mitochondrial fragmentation is closely linked to cell death mechanisms.
Drug Discovery and Screening: The selective action of P110 on mitochondrial fission machinery makes it a valuable candidate for high-content screening assays and drug discovery platforms targeting mitochondrial dysfunction. Researchers employ the peptide to validate mitochondrial fission as a therapeutic target and to screen for novel compounds with similar or complementary activities. Its defined mechanism of action provides a benchmark for assessing the efficacy and specificity of new molecular entities aimed at modulating mitochondrial dynamics.
Cellular Metabolism Investigations: The peptide is also employed in studies exploring the relationship between mitochondrial morphology and cellular energy metabolism. By altering the balance of fission and fusion, P110 offers researchers a means to probe how changes in mitochondrial structure affect ATP production, metabolic flux, and bioenergetic efficiency. These investigations are crucial for understanding the metabolic adaptations that occur in response to stress, disease, or genetic manipulation, and for identifying potential metabolic vulnerabilities associated with altered mitochondrial dynamics.
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