LTX-315 is an oncolytic peptide with potent anticancer activity; inhibits MRC-5, A20 and AT84 with IC50s of 34.3, 8.3 and 11 μM, respectively.
CAT No: R1491
CAS No:1345407-05-7
Synonyms/Alias:LTX-315;1345407-05-7;Oncopore;Ruxotemitide;Kkwwkkwdipk-nh2;ruxotemitida;Kkwwkkw-.beta.-phenyl-fk-nh2;LTX 315;RUXOTEMITIDE [INN];UNII-75FBL12IZ7;75FBL12IZ7;(S)-2,6-diamino-N-((5S,8S,11S,14S,17S,20S,23S,26S)-11,20,23-tris((1H-indol-3-yl)methyl)-1,30-diamino-14,17-bis(4-aminobutyl)-8-benzhydryl-5-carbamoyl-7,10,13,16,19,22,25-heptaoxo-6,9,12,15,18,21,24-heptaazatriacontan-26-yl)hexanamide;L-LYSINAMIDE, L-LYSYL-L-LYSYL-L-TRYPTOPHYL-L-TRYPTOPHYL-L-LYSYL-L-LYSYL-L-TRYPTOPHYL-.BETA.-PHENYL-L-PHENYLALANYL-;ruxotemitidum;CHEMBL4297628;LTX 315 [WHO-DD];KKWWKKW-BETA-PHENYL-FK-NH2;s8199;AKOS032945178;CCG-270681;CS-6979;DB12748;BS-15278;DA-65090;HY-19894;D84062;Q27266383;(2S)-6-AMINO-2-[(2S)-2-[(2S)-2-[(2S)-6-AMINO-2-[(2S)-6-AMINO-2-[(2S)-2-[(2S)-2-[(2S)-6-AMINO-2-[(2S)-2,6-DIAMINOHEXANAMIDO]HEXANAMIDO]-3-(1H-INDOL-3-YL)PROPANAMIDO]-3-(1H-INDOL-3-YL)PROPANAMIDO]HEXANAMIDO]HEXANAMIDO]-3-(1H-INDOL-3-YL)PROPANAMIDO]-3,3-DIPHENYLPROPANAMIDO]HEXANAMIDE;L-LYSINAMIDE, L-LYSYL-L-LYSYL-L-TRYPTOPHYL-L-TRYPTOPHYL-L-LYSYL-L-LYSYL-L-TRYPTOPHYL-BETA-PHENYL-L-PHENYLALANYL-;
LTX-315 is a synthetic oncolytic peptide derived from the bovine lactoferricin sequence, engineered to target and disrupt cancer cell membranes through a unique lytic mechanism. As a cationic amphipathic peptide, it exhibits high affinity for negatively charged phospholipids commonly found on the surface of malignant cells, distinguishing it from non-malignant tissues. Its mode of action involves rapid membrane permeabilization, leading to direct cytolysis and the release of intracellular components, which can subsequently trigger immunogenic cell death. Due to these properties, LTX-315 has gained significant attention as a tool for investigating tumor immunology, membrane biology, and peptide-mediated cytotoxicity in preclinical research settings.
Oncolytic peptide research: LTX-315 serves as a valuable molecular probe in the study of oncolytic mechanisms, enabling researchers to dissect the interactions between cationic peptides and cancer cell membranes. Its well-characterized sequence and rapid lytic activity facilitate mechanistic investigations into how amphipathic peptides selectively disrupt tumor cell integrity. Such studies are instrumental in advancing the understanding of peptide-membrane interactions, membrane composition differences between healthy and malignant cells, and the structural requirements for oncolytic selectivity.
Immunogenic cell death studies: The ability of LTX-315 to induce immunogenic cell death (ICD) makes it a critical reagent for elucidating the biochemical pathways involved in danger signal release and subsequent immune activation. When used in cellular models, it promotes the liberation of damage-associated molecular patterns (DAMPs) such as ATP, HMGB1, and calreticulin, providing a controlled system to study the molecular events that prime dendritic cells and initiate adaptive immune responses. This application is particularly relevant for researchers exploring the interface between cell death modalities and anti-tumor immunity.
Membrane permeabilization assays: The peptide's potent lytic properties are leveraged in membrane integrity assays, where it acts as a positive control or experimental agent to evaluate membrane disruption. Its amphipathic structure enables precise modulation of membrane permeability, making it suitable for studies involving liposome leakage, artificial membrane models, and quantitative assessments of cell membrane robustness. Such assays are foundational for understanding membrane dynamics and for screening other membrane-active compounds.
Peptide engineering and structure-activity relationship (SAR) analysis: LTX-315 is frequently employed as a template in peptide engineering studies aimed at optimizing oncolytic activity, selectivity, or pharmacokinetic properties. By systematically modifying its amino acid sequence or structural motifs, researchers can investigate the relationship between peptide structure and cytolytic efficacy. This approach aids in the rational design of next-generation oncolytic peptides and provides insight into the physicochemical determinants of peptide-membrane interactions.
Tumor microenvironment modeling: In advanced in vitro and ex vivo models, LTX-315 is used to simulate cytolytic events within the tumor microenvironment, enabling detailed exploration of how localized cell lysis influences stromal components, immune cell recruitment, and extracellular matrix remodeling. Such applications are essential for developing more physiologically relevant cancer models and for understanding the broader impact of oncolytic peptides on tumor architecture and immune landscape. By integrating LTX-315 into these experimental systems, researchers gain a powerful tool for dissecting complex tumor-host interactions and evaluating potential combinatorial strategies in preclinical oncology research.
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