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TuCeptin: Broad-Spectrum, Resistance-Proof Antimicrobial Peptides

Stopping Infections Where Traditional Antibiotics Fail

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Stopping Infections Where Traditional Antibiotics Fail

TuCeptin is a synthetically evolved antimicrobial peptide that sterilises all drug-resistant ESKAPE pathogens and their biofilms by rapidly lysing bacterial membranes . Unlike conventional antibiotics, it does not induce resistance or cross-resistance even after serial passage . D-amino formulations remain stable for more than five years lyophilised and over a year in saline at 4 °C, giving TuCeptin the shelf-life required for real-world deployment . In vivo, the peptide eradicates complex deep-wound infections caused by MRSA and MDR P. aeruginosa and show minimal cytotoxicity in a five-day topical dosing study . Independent work further validated the platform, with oral TuCeptin killing MDR E. coli and cured mouse enteritis while remaining highly stable and non-toxic.

Researchers

Why TuCeptin?

• Resistance-Proof Killing Mechanism

Rapidly disrupts bacterial membranes, leaving no opportunity for genetic escape—no resistance detected after serial passage of MDR isolates.

• Broad-Spectrum & Biofilm Power

Sterilises all ESKAPE pathogens and dismantles stubborn biofilms that shield chronic wounds, catheters, and implants.

• Validated In Vivo Efficacy

Cures deep-wound MRSA and MDR P. aeruginosa infections, and an independent 2025 study showed complete clearance of MDR E. coli enteritis in mice.

• Multi-Year Shelf Stability

D-amino peptide formulations remain potent for >5 years lyophilised and >12 months in saline at 4 °C.

• Low Mammalian Toxicity

Exhibits minimal cytotoxicity and no adverse local effects during repeated topical or systemic dosing.

• Scalable Synthesis

Short solid-phase build and simple purification streamline manufacturing; robust IP portfolio protects composition and clinical uses.

TuCeptin clusters at the bacterial cell membrane, rapidly killing the cell through a lysing mechanism. The minimum sterilizing concentrations remain well below the clinically useful MIC threshold (red line) across ESKAPE and other priority pathogens, indicating broad-spectrum potency at therapeutically achievable doses (bottom).

Bacteria quickly develop resistance against traditional antibiotics (top), but are unable to gain resistance to TuCeptin, even after multiple generations (bottom).

Publications

Optimization of Host Cell-Compatible, Antimicrobial Peptides Effective against Biofilms and Clinical Isolates of Drug-Resistant Bacteria View
Synthetic molecular evolution of host cell-compatible, antimicrobial peptides effective against drug-resistant, biofilm-forming bacteria View
The Remarkable Innate Resistance of Burkholderia bacteria to Cationic Antimicrobial Peptides: Insights into the Mechanism of AMP Resistance View

Other resources

BIO from the Bayou Podcast: Peptide Protectors - New Defenders in the Fight Against Superbugs with Key Opinion Leader Bill Wimley View
Title Country Date of Application Serial / ID Number Additional Notes
Peptide Compositions and methods of use thereof PCT 02/12/2021 PCT/US2021/018031 Nationalized to EPO, USA, AU, BR, CA, CN

Explore a Partnership

Flexible collaboration models available — Sponsored Research, Co-Development, Licensing.

For inquiries, contact:
Alexis Ducote, PhD
Business Development Associate
aducote@tulane.edu
337.540.4025

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James Zanewicz (+1 504.919.3800),

Alexis Ducote (+1 337.540.4025),

Carolyn Scofield (+1 504.881.4542).