FOXO4-DRI
Also known as: FOXO4 D-retro-inverso peptide
A D-retro-inverso peptide designed to disrupt the FOXO4–p53 interaction, studied as a senolytic in laboratory models.
Development status: Preclinical — laboratory and animal studies only
Identifiers and molecular characteristics
- CAS number
- Not verified
- Molecular formula
- Not verified
- Molecular mass
- Not verified
- Amino-acid sequence
- Not verified
- PubChem CID
- Not verified
Identifiers are published only with a source and a check date. Fields marked “not verified” have not yet been confirmed against a primary source — we show the gap rather than an unchecked figure. Always confirm against the certificate of analysis for the specific lot you hold.
Biological targets
- FOXO4–p53 protein–protein interaction
Mechanism of action
A retro-inverso design uses D-amino acids in reverse sequence order, producing a molecule with a similar side-chain topology to the parent peptide but far greater protease resistance. The intent is to disrupt a specific protein–protein interaction implicated in senescent cell survival.
Research evidence and its limits
Cell culture and mouse studies. No human trials known to this entry.
Safety considerations
No regulatory authority has assessed this compound as safe or effective for any human indication. The published record is predominantly laboratory and animal work, which does not establish human safety. Supplied and discussed here strictly as a laboratory research material. Not a medicine, not for human or veterinary administration, and nothing on this page should be read as a dosing, treatment or safety recommendation.
Analytical identification and quality testing
Identity by high-resolution mass spectrometry against the expected mass, purity by RP-HPLC with UV detection. Tandem MS sequencing or peptide mapping gives stronger identity evidence than mass alone.
Regulatory status
Not an approved medicine.
Frequently asked questions
What does "D-retro-inverso" mean?
The sequence is reversed and built from D-amino acids rather than the natural L form. The resulting side-chain arrangement resembles the original peptide while being largely invisible to proteases, which cleave L-peptides.
References
Related compounds
Entry last reviewed 2026-10-11. Regulatory status and scientific understanding change; verify against primary sources before relying on anything here.