Cardiotoxin Analog (CTX) IV (6-12) is a part peptide of Cardiotoxin Analog (CTX) IV. Cardiotoxin analogues IV isolated from the venom of Taiwan Cobra. CTX IV is an unique snake venom cardiotoxin.
CAT No: R1270
CAS No:115722-23-1
Synonyms/Alias:115722-23-1;Naja mossambica mossambica alpha-neurotoxin I;(2S)-1-[(2S)-1-[(2S,3S)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-3-methylpentanoyl]pyrrolidine-2-carbonyl]-N-[(2S)-1-[[(2S)-1-[[(2S)-1,6-diamino-1-oxohexan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]pyrrolidine-2-carboxamide;L-Leucyl-L-isoleucyl-L-prolyl-L-prolyl-L-phenylalanyl-L-tryptophyl-L-lysinamide;DTXSID30151175;L-Lysinamide, L-leucyl-L-isoleucyl-L-prolyl-L-prolyl-L-phenylalanyl-L-tryptophyl-;Cardiotoxin Analog (CTX) IV 6-12;Leu-Ile-Pro-Pro-Phe-Trp-Lys-NH2;DTXCID5073666;CTX IV (6-12);HY-P1902;DA-71940;MS-31680;CS-0097992;G12572;(S)-1-((S)-1-((2S,3S)-2-((S)-2-amino-4-methylpentanamido)-3-methylpentanoyl)pyrrolidine-2-carbonyl)-N-((S)-1-((S)-1-((S)-1,6-diamino-1-oxohexan-2-ylamino)-3-(1H-indol-3-yl)-1-oxopropan-2-ylamino)-1-oxo-3-phenylpropan-2-yl)pyrrolidine-2-carboxamide;
Cardiotoxin Analog (CTX) IV 6-12 is a synthetic peptide derivative modeled after naturally occurring cardiotoxins found in snake venom, specifically from the Naja naja atra species. Characterized by its defined amino acid sequence and stable secondary structure, CTX IV 6-12 represents a valuable tool for researchers investigating the structure-function relationships of cardiotoxins and their interactions with biological membranes. Its ability to mimic the functional domains of native cardiotoxins makes it particularly useful for dissecting the molecular mechanisms underlying membrane disruption, cytotoxicity, and protein-lipid interactions in a controlled experimental context. As a research-use peptide, CTX IV 6-12 enables the study of complex biochemical processes without the variability associated with crude venom extracts.
Membrane Interaction Studies: Due to its amphipathic structure and sequence similarity to native cardiotoxins, CTX IV 6-12 is frequently employed in research focused on the biophysical and biochemical properties of membrane-active peptides. Scientists use this analog to probe the mechanisms by which cardiotoxins interact with phospholipid bilayers, induce membrane permeabilization, and alter membrane dynamics. Such studies contribute to a deeper understanding of peptide-membrane recognition, pore formation, and the determinants of membrane selectivity, providing insights relevant to toxinology and membrane biology.
Protein Structure-Function Analysis: CTX IV 6-12 serves as a model system for elucidating the relationship between peptide sequence, three-dimensional conformation, and biological activity. By introducing specific sequence modifications or truncations, researchers can systematically evaluate the roles of individual residues and structural motifs in mediating cytotoxic effects or binding affinity to target membranes. This approach is instrumental in mapping functional domains and advancing rational peptide design for both fundamental and applied research.
Peptide Engineering and Design: The well-defined structure and functional attributes of CTX IV 6-12 make it a preferred scaffold for peptide engineering efforts. Scientists leverage this analog to develop novel peptides with tailored biological properties, such as enhanced stability, altered target specificity, or reduced off-target effects. Through site-directed mutagenesis or chemical modification, the analog provides a versatile platform for generating new research tools and exploring the principles of peptide-based molecular recognition.
Assay Development: CTX IV 6-12 is utilized in the development and validation of in vitro assays aimed at quantifying peptide-induced cytotoxicity, membrane disruption, or protein-lipid interactions. Its reproducible activity profile and defined sequence allow for consistent assay calibration and benchmarking, supporting the generation of reliable experimental data. These assays are essential for screening peptide libraries, evaluating structure-activity relationships, and characterizing the effects of pharmacological modulators on membrane-active peptides.
Comparative Toxinology: Researchers investigating the diversity and evolution of snake venom toxins employ CTX IV 6-12 as a reference compound for comparative studies. By analyzing its activity alongside other cardiotoxins and related peptides, scientists can assess the functional significance of sequence variations and gain insights into the adaptive strategies of venomous species. Such comparative analyses advance the broader understanding of toxin evolution, structure-function diversity, and the ecological roles of venom components.
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