Current treatment often controls the patient. N-BX01 is being designed to control the disease.
Endometriosis treatment frequently requires a compromise between pain control, hormonal function, fertility objectives, adverse effects and the possibility of lesion recurrence.
N-BX01™ is based on a different therapeutic proposition: identify a lesion-supporting intracellular signal, reach it with a precision peptide, interrupt its pathological nuclear activity, and allow the lesion to lose the biological programme that sustains it.
The objective is lesion regression without forcing the entire reproductive system into suppression.
N-BX01™ development profile
Development-stage descriptors. Molecular specifics are released responsibly, after protection and analytical confirmation.
Stopping the message before it becomes a disease programme
Design principle: preserve useful β-catenin biology; exclude pathological nuclear β-catenin activity.
Pathological activation
Disease-associated signalling increases the availability or activity of β-catenin within endometriosis cells.
Cytoplasmic accumulation
β-catenin escapes normal regulation and becomes available for nuclear transport.
Nuclear translocation
β-catenin enters the nucleus and participates in transcriptional complexes.
Lesion-supporting transcription
Genes associated with persistence, invasion, inflammatory signalling, tissue remodelling and fibrosis may become activated.
N-BX01 intervention
N-BX01 is being engineered to interfere selectively with a molecular step required for pathological nuclear β-catenin activity.
Biological resolution
Successful target engagement could reduce lesion fitness, diminish invasive behaviour and permit regression and clearance.
From molecular idea to physical peptide
The N-BX programme was initiated by Bogdan Dicoias as a mechanism-first peptide project.
The development route begins with identification of binding motifs and molecular interfaces capable of influencing β-catenin transport, retention or transcriptional interaction. Candidate sequences are evaluated computationally and prioritised by predicted target affinity, intracellular accessibility, conformational stability, proteolytic resistance, aggregation risk, solubility, chemical synthesizability and potential for lesion-directed activity.
Selected sequences enter solid-phase peptide synthesis and continuous-flow process development on SYNTHESERACT™ — Bogdan Dicoias's own CF-SPPS platform — to generate the first physical N-BX candidate family.
Only a candidate that passes proceeds to biology
Correct molecular identity · expected molecular mass · acceptable chromatographic purity · controlled impurity profile · reproducible synthesis · suitable solubility · formulation compatibility · stability under intended storage and use conditions.
The N-BX translational pathway
Each stage illuminates as a real milestone is reached; the stages ahead remain outlined.
Candidate discovery
Generation and ranking of the N-BX peptide series: can it bind the intended interface, enter the relevant cell, alter nuclear β-catenin activity — without broad cytotoxicity?
Cellular proof of mechanism
Uptake, intracellular localisation, nuclear-to-cytoplasmic β-catenin distribution, β-catenin-dependent transcription, migration/invasion, EMT markers, matrix production, inflammatory mediators, viability and selectivity.
Preclinical disease models
Lesion count and volume, histological activity, fibrosis and adhesions, inflammatory response, pain-associated behaviour, cycle preservation, biodistribution, pharmacokinetics and recurrence after withdrawal.
IND-enabling programme
Clinical-grade manufacturing, product specifications, formulation, repeat-dose toxicology, safety pharmacology, genotoxicity where applicable, local tolerance, PK/biodistribution modelling, starting-dose justification and protocol design.
A clinical path designed to answer the cure question
Study designs are illustrative of intent and remain subject to the final preclinical profile and regulatory strategy.
A first-in-human study would initially establish:
- Safety and tolerability
- Dose-limiting effects
- Systemic exposure
- Half-life and clearance
- Immunogenicity
- Hormonal & reproductive safety signals
- A biologically appropriate dose range
A single-ascending-dose and multiple-ascending-dose design could be used, subject to the final preclinical profile and regulatory strategy.
The first patient study could evaluate:
- Target-engagement biomarkers
- Lesion-associated inflammatory markers
- Pain signals
- Imaging feasibility
- Menstrual-cycle preservation
- Early evidence of lesion response
A randomised, controlled study designed to determine whether N-BX01 changes the underlying disease:
- Change in recognised endometriosis-associated pain measures
- Change in lesion burden by standardised imaging
- Reduction in analgesic use
- Inflammatory & fibrotic biomarkers
- Quality-of-life improvement
- Preservation of ovulation & cyclicity
- Durability after treatment completion
- Time to symptom or lesion recurrence
Determination of:
- Optimal treatment dose
- Optimal treatment duration
- Patient-selection strategy
- Durability of remission
- Requirement for retreatment
- Effect across endometriosis phenotypes
A larger confirmatory programme comparing N-BX01 with appropriate contemporary treatment pathways. The defining question:
Does a finite course of N-BX01 produce a durable clinical and biological outcome superior to continued symptom suppression?
A potential cure requires more than pain reduction
N-BX01 development distinguishes four levels — and the programme is intended to climb the entire hierarchy.
Symptomatic response
Pain improves while treatment continues.
Disease modification
Lesion biology and disease activity are measurably altered.
Durable remission
Improvement persists after treatment has ended.
Potential cure
Active lesions eliminated or rendered inactive, symptoms resolved, no continuing suppression required, and no clinically meaningful recurrence during extended follow-up.
Clinical endpoint architecture
Patient outcomes
- Non-menstrual pelvic pain
- Dysmenorrhoea
- Dyspareunia
- Dyschezia
- Fatigue
- Analgesic consumption
- Quality of life
- Daily-function impairment
Disease outcomes
- Lesion number
- Lesion dimensions
- Lesion activity
- Endometrioma volume
- Fibrosis
- Adhesion-related findings
- Inflammatory signatures
- Recurrence after withdrawal
Reproductive safety
- Cycle regularity
- Ovulatory function
- Ovarian-reserve markers
- Endometrial-receptivity research
- Pregnancy outcomes in long-term studies
Molecular outcomes
- Target engagement
- Nuclear β-catenin distribution
- Wnt-associated transcription
- EMT markers
- Fibrotic & matrix markers
“We are not trying to build a better way to live with endometriosis. We are trying to build a way out of it.”
N-BX01 began with the refusal to accept that suppression, surgery and recurrence must remain the permanent cycle of endometriosis care. The scientific challenge is formidable — the biological target must be reached selectively; the peptide must survive, enter the correct cells and alter a pathological intracellular event without disrupting essential healthy functions. But every transformative therapeutic begins as an unanswered question. N-BX01 is ours.
N-BX01 clinical study information
When clinical studies become authorised and open for recruitment, this section will provide the details below.
- Official study registration
- Study phase and design
- Participating locations
- Eligibility information
- Investigator contacts
- Recruitment status
- Participant information materials
- Published study results
Trending in the field
Endometriosis research and non-hormonal peptide therapeutics, tracked as they publish.
Recent developments in the field — refreshed 2026-10-16 by Panacea Bio Chem.
- Macrophage-centered immune-fibrotic persistence in endometriosis and adenomyosis: non-hormonal immunopharmacological targets — PubMed, 2026
- Modern methods of treating vaginal dryness and atrophy — PubMed, 2026 Jun
- Metabolic-epigenetic imprinting of macrophages in endometriosis: a working model for lesion persistence and treatment — PubMed, 2026
- Pain management strategies and their associations with quality of life and pain interference in women with chronic pelvic pain: A cross-sectional survey — PubMed, 2026 Jan-Dec
The first goal is a molecule. The next is a medicine. The ultimate goal is an end to endometriosis.
Powered by NBetaX™ Nuclear β-Catenin Exclusion Technology
Frequently asked
What are peptides?
Peptides are molecules made from two or more amino-acid residues joined by peptide bonds. In everyday biomedical use, the term usually refers to amino-acid chains smaller than proteins, although the exact size boundary is not absolute. Their biological activity depends on sequence, structure and chemical modifications rather than on the word “peptide” alone. — sources: IUPAC Gold Book — peptides, NCBI MeSH — Peptides, NCBI/NCI — peptide definition
How do peptides work in the body?
Many endogenous peptides act as signalling molecules. They bind to receptors, enzymes, membranes or other molecular partners and change cellular behaviour such as hormone release, metabolism, inflammation, growth or tissue signalling. Different peptides can have completely different targets, so “peptides” should never be treated as one biological effect. — sources: Nature Reviews Drug Discovery — Trends in peptide drug discovery, AAMC — 10 questions to ask your doctor about peptides, Tufts Medicine — Peptides explained
What is the difference between peptides and proteins?
Both peptides and proteins are built from amino acids. Peptides are generally shorter chains, while proteins are usually longer and more likely to adopt complex three-dimensional structures. The boundary is conventional rather than absolute, so sequence length alone does not fully determine whether a molecule is called a peptide or protein. — sources: NCBI MeSH — Peptides, Nature Reviews Drug Discovery — Trends in peptide drug discovery
Are peptides steroids?
No. Peptides are amino-acid chains linked by peptide bonds, whereas steroids are molecules built around a characteristic four-ring carbon framework. Some peptides and some steroids can influence overlapping physiological systems, which is why they are sometimes discussed together, but chemically they are very different classes of molecule. — sources: IUPAC Gold Book — peptides, Harvard Health — Peptides: benefits and safety concerns
Are peptides hormones?
Some peptides are hormones, but many are not. Insulin, glucagon, oxytocin and many other signalling molecules are peptide hormones, while other peptides function as neurotransmitters, growth factors, antimicrobial molecules, research probes or synthetic drug candidates. “Peptide” describes chemistry; “hormone” describes biological function. — sources: Nature Reviews Drug Discovery — Trends in peptide drug discovery, AAMC — 10 questions to ask your doctor about peptides
Are peptides the same as amino acids?
No. Amino acids are the individual molecular building blocks. Peptides are formed when two or more amino-acid residues are joined, typically through peptide bonds. A peptide’s properties emerge from the sequence, length, charge, conformation and modifications of its component residues. — sources: IUPAC Gold Book — peptides, NCBI MeSH — Peptides
What is a peptide bond?
A peptide bond is the amide linkage that connects the carbonyl carbon of one amino-acid residue to the nitrogen of another. Repeating peptide bonds create the backbone of peptide chains. The sequence and side chains attached to that backbone determine much of a peptide’s chemistry and biological recognition. — sources: IUPAC Gold Book — peptides
How many amino acids are in a peptide?
There is no universally rigid cutoff. Peptides contain at least two amino-acid residues; terms such as oligopeptide, polypeptide and protein overlap, and different fields use somewhat different length conventions. It is better to state the actual sequence length than rely on a single arbitrary peptide/protein boundary. — sources: NCBI MeSH — Peptides, IUPAC Gold Book — peptides
Are peptides natural or synthetic?
Both. Living organisms produce many peptides naturally, while laboratories can synthesize identical sequences, analogues or entirely designed sequences. Synthetic chemistry also allows non-natural amino acids, cyclization, lipidation and other modifications that can alter stability, potency or pharmacokinetics. — sources: Nature Reviews Drug Discovery — Trends in peptide drug discovery, PubMed — Fmoc Solid-Phase Peptide Synthesis
Why can two peptides have completely different effects?
A change in amino-acid sequence can alter charge, shape, receptor affinity, stability and cellular distribution. Even closely related peptides can therefore engage different targets or behave differently in solution and in vivo. Sequence and structure, not the generic label “peptide,” determine function. — sources: Nature Reviews Drug Discovery — Trends in peptide drug discovery, PubMed — Factors affecting peptide aggregation
