BAX Inhibiting Peptide V5 protects Bax against conformational changes and it also prevents mitochondrial translocation. In vitro analysis prove that peptide V5 prevents apoptosis, mediated by a number of agents including staurosporine, ultraviolet, and anti-cancer drug.
CAT No: R1852
CAS No:579492-81-2
Synonyms/Alias:Bax inhibitor peptide V5;579492-81-2;Val-Pro-Met-Leu-Lys;(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-amino-3-methylbutanoyl]pyrrolidine-2-carbonyl]amino]-4-methylsulfanylbutanoyl]amino]-4-methylpentanoyl]amino]hexanoic acid;BIP-V5;BIP-V5;BAX Inhibiting Peptide V5;Bax inhibitor peptide V5?;HY-P0081;BAX Inhibiting Peptide V5; BIP-V5;AKOS024456777;CS-5509;DA-61502;D83676;
Chemical Name:(S)-6-amino-2-((Z)-((S)-2-((Z)-((S)-2-((Z)-(((S)-1-((S)-2-amino-3-methylbutanoyl)pyrrolidin-2-yl)(hydroxy)methylene)amino)-1-hydroxy-4-(methylthio)butylidene)amino)-1-hydroxy-4-methylpentylidene)amino)hexanoic acid
Bax inhibitor peptide V5 is a synthetic peptide designed to modulate the activity of Bax, a pro-apoptotic member of the Bcl-2 protein family that plays a central role in the regulation of programmed cell death. By mimicking or interfering with specific domains of Bax, this peptide enables targeted investigation of mitochondrial membrane permeabilization and the molecular mechanisms underlying apoptosis. Its sequence and structure are optimized for research applications, making it a valuable tool for dissecting protein-protein interactions and signaling pathways that govern cellular fate decisions in various biological contexts.
Apoptosis research: Bax inhibitor peptide V5 is widely utilized in studies focused on elucidating the molecular mechanisms of apoptosis. By selectively inhibiting Bax-mediated mitochondrial outer membrane permeabilization, the peptide allows researchers to investigate the downstream consequences of blocking this critical step in the apoptotic cascade. This capability is particularly valuable for distinguishing the specific roles of Bax versus other Bcl-2 family members in cell death pathways, facilitating a deeper understanding of apoptosis regulation in both physiological and pathological conditions.
Protein-protein interaction studies: The peptide serves as a functional probe for characterizing interactions between Bax and its binding partners, such as anti-apoptotic proteins like Bcl-2 and Bcl-xL. Through competitive binding assays or co-immunoprecipitation experiments, researchers can employ the inhibitor to map interaction domains, assess binding affinities, and delineate the structural determinants required for complex formation. These insights contribute to the broader understanding of how Bcl-2 family dynamics control mitochondrial integrity and cellular survival.
Cellular stress response analysis: Bax inhibitor peptide V5 is instrumental in exploring cellular responses to various stressors, including oxidative damage, DNA insults, and endoplasmic reticulum stress. By modulating Bax activity, the peptide aids in distinguishing apoptosis-dependent from apoptosis-independent mechanisms of cell death and adaptation. This enables more precise dissection of signaling networks involved in stress adaptation, providing valuable information for studies on cellular resilience and vulnerability.
Drug discovery and screening: In the context of early-stage drug discovery, the peptide is employed as a reference or control compound in high-throughput assays designed to identify novel modulators of Bax function. Its well-characterized inhibitory effects provide a benchmark for evaluating the potency and specificity of small molecules or biologics targeting the apoptotic machinery. This application supports the rational design and optimization of apoptosis modulators for research use in oncology, neurobiology, and immunology.
Mitochondrial biology research: Bax inhibitor peptide V5 is also used to investigate the role of mitochondrial membrane dynamics in cell fate determination. By preventing Bax-induced mitochondrial permeabilization, the peptide allows for the study of mitochondrial physiology under conditions where apoptotic signaling is selectively suppressed. This approach is valuable for unraveling the interplay between mitochondrial function, energy metabolism, and cell death pathways, offering insights into fundamental aspects of cell biology and disease mechanisms.
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