Synthetic D-Retro-Inverso Senolytic Peptide — Research Peptide
$119.00
FOXO4-DRI supplied as a lyophilized laboratory peptide reference material for controlled protein-interaction and cell-model research. Research use only. Not for human or veterinary use.
Reference characteristics for laboratory research materials.
CAS Number
2460055-10-9
Purity
≥98%
Molecular Formula
C228H388N86O64
Molecular Weight
5358.06
Appearance
White lyophilized powder
Storage
-20°C
Research Classification
Research Use Only (RUO). Not for human or veterinary use.
SCIENTIFIC OVERVIEW
Scientific background and research classification for this laboratory reference material.
FOXO4-DRI (FOXO4 D-Retro-Inverso) is a synthetic senolytic research peptide built from all-D amino acids in a retro-inverso configuration, derived from the FOXO4 region that engages p53 and fused to a cell-penetrating (arginine-rich) segment. CAS 2460055-10-9; molecular formula C228H388N86O64. It is supplied as a lyophilized peptide reference material for laboratory research use only.
The D-retro-inverso chemistry (all-D residues, reversed sequence) is intended to confer protease resistance while approximating the interaction surface of the parent sequence. FOXO4-DRI is a distinct synthetic peptide entity and is not the native FOXO4 protein.
Primary Research Category
Longevity & Cellular Health
Material Type
Lyophilized Peptide
Intended Use
Laboratory Research
Research Categories
LongevityCellular SenescenceHealthy Aging
Mechanism of Action
Molecular interaction profile describing how this research material engages receptor systems and influences downstream biological signaling pathways.
FOXO4-DRI is reported to act by engaging p53: structural work identifies the disordered p53 transactivation domain as the binding target of FOXO4 and of FOXO4-DRI (Bourgeois et al., 2025). In senescent-cell models the peptide is reported to promote nuclear exclusion of p53 and to induce apoptosis selectively in senescent cells (Baar et al., 2017; Kong et al., 2025). The direct molecular target is the p53 transactivation domain, which is not represented in the governed molecular-target vocabulary; the governed molecular-target and pathway fields are therefore left empty by design, and 'FOXO' — the family the peptide is derived from — is not asserted as a target.
Biological Pathways
Apoptosis
Research Documentation
Laboratory documentation is presented when available for the selected product specification and current lot.
In Laboratory Testing
Laboratory Documentation In Progress
Identity
Purity
Endotoxin
Fentanyl
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Research Center
Scientific literature, laboratory resources, and related materials curated to support research involving this research material.
Scientific References
Peer-Reviewed Literature
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Comprehensive scientific documentation including literature review, mechanism, pharmacology, and study data for this research material.
Laboratory Resources
Technical Guidance
Storage guidance, handling information, analytical standards, research policies, and laboratory support documentation.
Research Library
Curated peer-reviewed literature selected to provide scientific context for this research material.
Preclinical Study•Cell•2017
Targeted Apoptosis of Senescent Cells Restores Tissue Homeostasis in Response to Chemotoxicity and Aging
Foundational report introducing the FOXO4-based D-retro-inverso senolytic peptide and showing that targeted apoptosis of senescent cells restores tissue homeostasis in models of chemotoxicity and aging — the discovery/origin of FOXO4-DRI.
Velora Research Insight
Discovery/origin of FOXO4-DRI as a senolytic. de Keizer/Bourgeois originating lineage. In-vitro and animal-model evidence; foundational, not human-efficacy evidence.
The disordered p53 transactivation domain is the target of FOXO4 and the senolytic compound FOXO4-DRI
Structural/mechanistic study identifying the disordered p53 transactivation domain as the direct binding target of FOXO4 and of FOXO4-DRI, clarifying the molecular basis of the peptide's activity.
Velora Research Insight
Defines the direct molecular target as the p53 transactivation domain — the evidentiary basis for molecular_targets=[] (p53 not in governed vocabulary; 'FOXO' is origin, not target). Shares the de Keizer/Bourgeois originating lineage (not an additional independent lineage).
FOXO4-DRI induces keloid senescent fibroblast apoptosis by promoting nuclear exclusion of upregulated p53-serine 15 phosphorylation
Independent preclinical study reporting that FOXO4-DRI induces apoptosis of keloid senescent fibroblasts by promoting nuclear exclusion of p53, corroborating the p53-nuclear-exclusion senolytic mechanism in an independent model.
Velora Research Insight
Fully independent application (no de Keizer overlap) corroborating the p53-nuclear-exclusion / senescent-cell-apoptosis mechanism in a distinct disease model. Preclinical, model-specific.
Review Article•Naunyn-Schmiedeberg's Archives of Pharmacology•2026
Targeting the FOXO4-p53 axis by retro-inverso peptide senolytic agents: a pharmacological strategy to mitigate brain aging and cognitive decline
Independent review synthesizing the FOXO4-p53 axis and retro-inverso peptide senolytics, discussing their proposed pharmacology in the context of aging research.
Velora Research Insight
Fully independent recent synthesis (no de Keizer overlap) situating FOXO4-DRI within FOXO4-p53-axis senolytic research. Carried as evidence-scoped context; its aging/cognition discussion is not a product efficacy claim.