Tell us the property that is holding your peptide back
Affinity is rarely what stops a peptide program. A sequence that binds well can still be cleared within minutes, shut out of its target compartment, or flagged in safety screening. Each of those has a chemical answer, and we run all five of them on this site.
Bring us your peptide challenge.
It is gone before it works
We take out what the proteases read
Non-natural amino acids and backbone edits remove the recognition sites, position by position, so stability arrives without costing you the activity.
It does not last between doses
We move exposure from hours to weeks
Fatty acids, cholesterol and PEG chains promote plasma protein binding against renal clearance, with the linker designed for your dosing interval.
It cannot reach the target
We engineer the molecule across the membrane
Conformational constraint and lipidation raise passive permeability, and the gain is confirmed in assay rather than assumed.
It aggregates, or will not dissolve
We read the physical behavior before scale-up
Salt form, physicochemical profiling and NMR pick up oligomerization and chemical instability while the series is still cheap to change.
It flags in safety screening
We catch the pseudo-allergic response in vitro
A mast cell degranulation assay on the hLAD2 line detects histamine release early, before it costs you an in vivo study.
A peptide reaches a candidate through a sequence of deliberate changes
Every modification answers a specific property
Starting sequence
A program starts from a binder recovered in a display selection, from a natural ligand or hormone, or from a sequence you already hold. Selection conditions reflect the physiological environment, so binders carry functional relevance before chemistry begins.
Selection runs on Peptide Phage Display and mRNA Display
Scan and design
Scan and design identify positions critical for activity and stability, and those that can be modified without losing function.
Design support from Computational Chemistry
Non-natural amino acids
More than 2,000 non-natural amino acids are held in-house and re-stocked routinely. When a design requires chemistry that no catalog can provide, novel amino acids, building blocks and multifunctional linkers can be synthesized ad hoc.
Backbone modification
Backbone modifications help control secondary structure, introduce crosslinks, or create anchoring points for subsequent substitutions.
Conformational constraint
Cyclization restricts the conformations a peptide samples, pre-organizing it for binding. The lower entropic penalty improves affinity, potency, selectivity and stability at once.
Conjugation
We derivatize peptides with the moiety required by the program, including fatty acids, diacids, cholesterol and PEG for half-life extension, as well as chelators, fluorescent labels and carrier proteins for targeting, imaging and theranostic applications. For each conjugation strategy, we also select the optimal linker or spacer, which can be synthesized ad hoc to match the required payload, positioning and application.
Candidate profile
Potency, selectivity, metabolic stability and exposure are measured on the same series in parallel. A change that buys one property and costs another shows up in the same round it was made.
Profiling runs with ADME & Pharmacology and Assay Development
Developability is measured from the early phase
Permeability, metabolic stability and aggregation enter the cascade alongside potency rather than after it. A liability found during lead optimization is expensive, and it is largely avoidable.
Physicochemical profile
Solubility, aggregation and chemical stability, with NMR and circular dichroism reading conformation in solution.
In vitro stability
Soft spot identification in biological matrices, with metabolite identification by high resolution mass spectrometry.
Exposure
Permeability assays, plasma protein binding and pharmacokinetics in relevant species, with label-free binding kinetics alongside.
Early derisking
Mast cell degranulation assay to flag peptide-driven pseudo-allergic reactions linked to histamine release.
Our integrated approach
Our fully integrated research site accelerates drug discovery through expert multi-parameteric optimization, cutting-edge analytical tools, and agile strategies.
Structure-based design supported by computer-aided drug design (CADD): targets design to support SAR elucidation based on structural information by modelling and test results. Monitoring of the physicochemical properties and early identification of possible chemical liabilities related to molecules structural class.
Designing optimal chemical routes. Utilizing parallel synthesis to rapidly produce structural analogs.
Test in primary and secondary assays · ADME · In vivo PK studies · Structural biology
Leveraging data from multiple sources to drive the next optimization step
Data from the Analyze stage informs the subsequent Design phase, iterating until the chemical series aligns with its target profile or is deprioritized.
The ultimate goal of our optimization pipeline is rigorous candidate selection. By balancing potency, selectivity, in vitro and in vivo ADME properties, and safety profiles, a series is advanced once it fully aligns with the Target Product Profile (TPP).
Inside the peptide chemistry facility
Synthesis, purification, analytical characterization and structural work run at a single research site in Rome, Italy.
Move faster from target to preclinical candidate
IRBM’s Integrated Drug Discovery platform unites chemistry, biology, DMPK, and in vivo pharmacology under one scientific framework so candidates advance through fewer handoffs, stronger data continuity, and better-informed decisions.
Frequently Asked Questions
What targets are best suited to peptide and macrocyclic peptide discovery?
Targets with extended or shallow binding surfaces, particularly protein-protein interactions, allosteric sites, and intracellular targets where cell permeability is required. Conformational constraint allows precision binding across a surface that small molecules often cannot cover.
When should developability filters enter a peptide program?
At hit stage. Assessing permeability, metabolic stability and aggregation early prevents investment in leads that carry inherent liabilities, and aligns discovery output with real development requirements.
Can IRBM start from a sequence we already have?
Yes. A program can start from a display hit, from a natural ligand or hormone, or from a sequence you supply. Work can also begin at a single question, such as a stability problem or a permeability problem, without committing to a full program.
How long a peptide can IRBM synthesize?
Sequences above 100 residues assemble by microwave-assisted solid-phase synthesis. Around 150 residues with disulfide bridges are reached by native chemical ligation with desulfurization, followed by refolding.
Where is the work carried out, and how is material handled?
At a single research site in Rome, Italy, on the former MSD Research Laboratories campus. Synthesis, purification, analytical characterization, structural biology, DMPK and in vivo pharmacology sit on the same site. Material and data do not change hands between organizations. Every compound is registered with a unique identifier in the IRBM database and in yours.
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