Lancovutide
A bacterial antibiotic peptide breathed in to make cystic fibrosis airways secrete chloride
Lancovutide is the clinical name for duramycin, a 19-amino-acid peptide made by a soil bacterium and known to chemists since the 1950s. It sticks to one particular membrane lipid, phosphatidylethanolamine, and in doing so disturbs the surface of any cell whose outer face carries that lipid. In the airway that disturbance makes epithelial cells secrete chloride, and chloride secretion is exactly what fails in cystic fibrosis. Because the peptide works without the broken CFTR protein, it was developed as an inhaled drug that might rehydrate the mucus of anyone with the disease, whatever their mutation. It got through a nasal study, a six-volunteer pharmacokinetic study and a 24-patient trial that showed a lung-function gain at the top dose. Then a 161-patient trial found nothing, and the programme stopped. The same molecule is still widely used in laboratories as a tag for phosphatidylethanolamine, and that second life accounts for most of what has been published about it.
Used in human trials: 2.5 mg, Once a day, every other day, or twice a week (three arms), Inhaled (nebulised) (Study: the 161-patient phase 2 trial) Details ↓
Recommended Dosing
Used in human trials
No manufacturer dose exists for this use: these are amounts given in published trials, not recommendations.
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What is it?
Duramycin came out of a screen of soil bacteria for antibiotics, and for forty years that was all it was: a small, extremely stable peptide from Streptomyces with modest activity against gram-positive bacteria and an odd chemical structure. It belongs to the lantibiotics, peptides whose amino acids are stitched together after synthesis into rings through sulfur bridges, the same family as nisin, the preservative in processed cheese. Duramycin carries four such rings, including an unusual bridge between a lysine side chain and a serine, and a hydroxylated aspartate. The 1990 structure paper found that the molecule had been drawn wrongly in the earlier literature and that it differs from the related peptide cinnamycin by a single residue.
What made it a drug candidate was an experiment on dog windpipe. In 1990 a group mounted canine tracheal tissue in a chamber and found that adding duramycin to the side facing the airway raised the electrical current across it, entirely because the tissue started secreting chloride. The effect needed no cyclic AMP, the usual second messenger for chloride secretion, and it did not depend on the sodium channel. Chloride secretion is what collapses in cystic fibrosis, where mutations in the CFTR gene leave the main chloride channel absent or shut; the airway surface dries out, mucus thickens, and lungs fill with infection. Here was a molecule that seemed to open a different route altogether, which would make it useful to every patient regardless of mutation.
The clinical programme ran under the code Moli1901 and later the name lancovutide. Animal work established that an inhaled dose stays where it lands: radiolabelled peptide given to rats and to beagle dogs sat in lung tissue for weeks and barely entered the blood. A first study in people superfused it through the nose in four volunteers and four patients and measured the electrical potential across the nasal lining, which shifted in a way consistent with increased chloride transport, more briefly in the patients than in the healthy volunteers. Six healthy men then inhaled a single 7.5 mg dose and had bronchoscopies: the peptide was still measurable in their airway cells many days later, was undetectable in plasma, and raised none of fourteen inflammatory signals in lavage fluid.
The 2007 trial was the encouraging one. Twenty-four adults with stable cystic fibrosis inhaled 0.5, 1.5 or 2.5 mg a day for five days, and the group at the highest dose came out with better FEV1 than placebo. One person's FEV1 dropped sharply after inhaling and recovered on its own; another had a numb throat during dosing. The authors described the total 12.5 mg exposure as safe and worth pursuing. What followed was a proper test: 161 patients aged 12 and up, four groups, inhaled 2.5 mg daily, every other day or twice a week against saline for eight weeks. Nothing separated the groups on lung function, quality of life, exacerbations or additional treatment, and respiratory side effects were more common on the drug than on placebo. No further trial of the peptide has been registered.
The pharmacology probably explains the disappointment. Later cell work argues that duramycin does not open a specific chloride channel so much as make the membrane leak. In cultured human colonic epithelium it created large, barely selective conductances; in artificial membranes it formed channels that grew and merged over time until the membrane failed; in cystic fibrosis bronchial cells chloride efflux rose only in a narrow band around one micromolar and was blocked at higher concentrations. A window that narrow is hard to hold in a human lung, and a drug whose action is membrane disturbance has little room between doing something and doing harm. The peptide's affinity for phosphatidylethanolamine, meanwhile, turned out to be so clean that laboratories adopted it as a reagent: coupled to a chelator and a radioactive metal it marks dying cells, which is why most duramycin papers published since 2008 are imaging papers about a different product entirely.
Mechanism of Action
Lancovutide binds one membrane lipid, phosphatidylethanolamine, and disturbs the membrane it lands on. In the airway that disturbance lets chloride out and calcium in; in a bacterium it breaks the cell envelope; in a laboratory it makes a convenient tag for dying cells.
Binds phosphatidylethanolamine, and only that
The peptide binds ethanolamine phospholipids one to one, ignores phosphatidylcholine, and prefers tightly curved membranes, which it then deforms further (PMIDs 17483159, 1741778).
Opens the airway surface to chloride
Added to the airway face of tracheal tissue in a narrow concentration band it raises short-circuit current entirely as net chloride secretion, without cyclic AMP and without CFTR, which is why cystic fibrosis was the target (PMIDs 2169195, 21091780).
Raises calcium inside the cell
In tracheal cells it pushes free calcium from tens of nanomolar to around a micromolar, from internal stores and from outside; chelating that calcium blunts the chloride secretion, and blocking protein kinase C blunts the secretion without touching the calcium (PMID 8361390).
Makes non-selective openings as it accumulates
In artificial membranes and in epithelial patches the conductance it creates grows and merges over time into large, weakly anion-selective pores, and in colonic epithelium most of the resulting current is sodium rather than chloride, so the useful window between an effect and a leak is narrow (PMIDs 1377492, 1762061).
Kills gram-positive bacteria with the same lipid
Susceptibility tracks phosphatidylethanolamine in the bacterial membrane, resistant mutants have lost or replaced that lipid, and treated cells visibly change at the envelope (PMIDs 29491859, 2933071, 2921248).
Published Research
The studies below were read from their PubMed abstracts in November 2026: the four human studies, the animal pharmacokinetic work in rats, mice and dogs, the epithelial experiments that made the drug a candidate, the membrane chemistry that explains what it does, and one recent review. Duramycin is also the backbone of a family of radiolabelled cell-death imaging probes, and those are different products under our rule that a card follows the molecule tested, so they are listed under References. Three cards are for papers whose titles name the condition or the lipid rather than the peptide; each carries a relevance-sweep record quoting the words in its abstract that name it.
First study in people: nasal superfusion
Four volunteers without cystic fibrosis and four patients with it had the peptide, or placebo, run across the lining of the nose at rising concentrations from 0.01 to 10 micromolar, while the electrical potential across that lining was recorded every minute. Nothing visible happened to the nose, lavage fluid showed no sign of damage, and lung function did not change. The potential shifts suggested both an immediate and a lasting increase in chloride transport in the volunteers, with a dose relationship; in the patients the immediate response faded faster and no clear dose relationship emerged from four people.
Phase 2: five days inhaled, a gain at the top dose
Twenty-four adults with stable cystic fibrosis at one centre inhaled 0.5, 1.5 or 2.5 mg a day for five consecutive days, or placebo, in a double-blind rising-dose design. FEV1 improved significantly against placebo in the 2.5 mg group. Tolerance was good in all but two patients: one had a transient sharp fall in FEV1 after inhaling that resolved by itself, and one had passing numbness of the throat while inhaling. The drug was not detectable in the plasma of the highest-dose group. The authors concluded that a cumulative 12.5 mg was safe and that the lung-function effect justified efficacy trials.
Where an inhaled dose goes, and for how long
Six healthy men each inhaled one nebulised 7.5 mg dose and then underwent bronchoscopy, so that the peptide could be measured in the cells of lavage fluid, mostly alveolar macrophages, and in brushings of bronchial lining. Its estimated half-life was about five days in the brush samples and between 25 and 91 days in lavage cells, where the peak concentration was roughly twenty times higher. None reached plasma, and a panel of fourteen cytokines in lavage fluid showed no inflammatory reaction. The authors read this as support for giving the peptide into the lung in cystic fibrosis.
The trial that ended the programme
In a multi-centre, double-blind, placebo-controlled trial, 161 patients aged 12 and over with confirmed cystic fibrosis were assigned to saline or to 2.5 mg inhaled once a day, every other day, or twice a week, for eight weeks. The main measurement, change in FEV1 as a percentage of predicted, did not differ between groups, and neither did other lung-function measures, quality of life, pulmonary exacerbations, hospital admission, time to first exacerbation or the need for extra anti-inflammatory, mucolytic or antibiotic treatment. Inhalation was described as safe overall, though adverse events, particularly respiratory ones, were more frequent on the drug than on placebo.
Pharmacokinetics in rats and mice
Radiolabelled peptide given to rats as an aerosol deposited heavily in the respiratory tract and stayed there almost unchanged for seven days, with next to nothing in the bloodstream. Given by mouth it was barely absorbed and was almost entirely in the faeces within two days. Given into a vein, rats had excreted 54 per cent in faeces and 5 per cent in urine by day seven, with 44 per cent still in the body and most of that in the liver. After instillation into the windpipe, clearance from the lung had a half-life of 64 days and plasma concentrations stayed below one nanogram-equivalent per millilitre throughout. Mice behaved like rats.
Dog study with a very small radioactive dose
Carbon-14-labelled peptide, about 100 micrograms, was instilled into one lung lobe of beagles and tracked by accelerator mass spectrometry, a technique sensitive enough to use a dose of radioactivity far below the usual. Sixty-four per cent of the dose was still in that lobe 28 days later. Blood levels stayed under 5 ng/mL at all times, and concentrations in other lung lobes, liver, kidney, spleen, brain and bile never reached a quarter of one per cent of the dosed lobe. About 13 per cent of the dose left the body in 28 days, mostly in faeces. The pattern matched rats and mice: slow in, slow out, no accumulation elsewhere.
The experiment that started the programme
Canine tracheal tissue was mounted in chambers and duramycin added to the solution bathing the airway side. Over a narrow range of concentrations it raised short-circuit current and net chloride secretion, peaking at two micromolar, with no change in the flux of mannitol, which argues against simple leakiness at that dose. Higher concentrations reduced the current instead. Adding it from the other side did nothing except at high concentrations. Blocking sodium transport with amiloride first did not change the response, and tissue already stimulated with a cyclic AMP analogue responded as strongly as untreated tissue, so the peptide works through some pathway other than cyclic AMP.
A large rise in calcium inside airway cells
In suspensions of bovine and canine tracheal cells, duramycin raised free intracellular calcium from about 34 nanomolar to roughly 950 nanomolar at five micromolar, both by releasing calcium from internal stores and by letting it in from outside. Chelating calcium inside the cells blunted both the calcium rise and the chloride secretion. A protein kinase C inhibitor blunted the secretion while leaving the calcium rise intact, which tells you that calcium alone is not enough to make these cells secrete chloride. Human neutrophils showed no calcium response at all.
In gut epithelium the current is mostly sodium, through artificial pores
Duramycin and the related peptide cinnamycin were applied to cultured human colonic epithelium. Both acted only from the apical side and both raised transport current, but above two to five micromolar the current either collapsed or became large and unstable. Ion-substitution experiments showed that most of the current was electrogenic sodium absorption rather than chloride secretion, and duramycin produced huge 2,000-picosiemens conductances in artificial lipid films. The authors found no evidence that either peptide acts on a specific channel or receptor, and proposed that they make non-selective openings in the membrane instead.
A narrow working window in cystic fibrosis cells
Chloride efflux and intracellular calcium were measured in cystic fibrosis and non-cystic-fibrosis epithelial lines. Duramycin raised chloride efflux from cystic fibrosis bronchial cells only around one micromolar; at 100 and 250 micromolar it blocked efflux. Both a CFTR inhibitor and a blocker of calcium entry suppressed the response. No effect appeared in non-cystic-fibrosis bronchial cells, in airway gland cells or in pancreatic cells of either kind. Calcium went up in the non-cystic-fibrosis line and down in the cystic fibrosis line. The authors read the whole pattern as non-specific membrane disturbance rather than activation of a calcium-activated chloride channel.
The channels it makes grow and merge
In artificial black lipid membranes and in patches of human colonic epithelial cells, duramycin produced erratic conductance that partly resolved into steps and partly did not. Both the total conductance and the size of individual steps increased with time. The channels were weakly selective for anions, and the smaller ones in cell patches rectified inward. Less peptide was needed when the artificial membrane contained phospholipid rather than a neutral lipid, and less again in living cells than in bilayers. The authors concluded that peptide accumulates, small openings coalesce into larger ones, and the membrane eventually breaks down.
What it binds, and why curvature matters
Duramycin and cinnamycin were tested against a range of membrane lipids. Both bound ethanolamine phospholipids and nothing else, and both bound small vesicles far better than large ones, so the recognition depends on how tightly the membrane is curved. Binding to multilayered vesicles pulled them into tubes, which electron microscopy and small-angle X-ray scattering both showed. The authors suggest the peptides help their own binding along by deforming the membrane they land on.
Which bacteria it kills, and how
Duramycin was screened against bacterial isolates taken from poplar trees to see what it does and does not kill. Comparing the membrane lipids of susceptible and resistant strains showed that a gram-positive bacterium is sensitive when its membrane contains phosphatidylethanolamine. High-resolution atomic force microscopy of treated cells showed the cell envelope changing step by step in the susceptible strains. The work ties the peptide's antibacterial selectivity to the same lipid that explains everything else it does.
It blocks phospholipase A2 by hiding the substrate
Duramycin, duramycin B and C and cinnamycin each inhibited phospholipase A2 from six different sources with half-maximal concentrations around one micromolar, but only when the substrate offered was phosphatidylethanolamine, or bacterial membrane rich in it. With phosphatidylcholine there was no inhibition. Pre-incubating the peptide with phosphatidylethanolamine vesicles abolished the effect, and circular dichroism showed the peptides changing shape on binding that lipid and not on binding phosphatidylcholine. The inhibition is therefore indirect: the peptide sequesters the enzyme's substrate rather than touching the enzyme.
Early membrane work, and the first resistant bacteria
Low concentrations of duramycin made lipid vesicles containing unsaturated phosphatidylethanolamine clump together, as did vesicles from rabbit muscle sarcoplasmic reticulum, and the peptide blocked ATP-driven calcium uptake into those vesicles without affecting ATP breakdown or calcium permeability. A reconstituted bacterial proton pump was inhibited only when the surrounding lipid contained phosphatidylethanolamine. The authors also isolated a resistant strain of Bacillus subtilis, mapped the resistance, and found no detectable phosphatidylethanolamine in its membrane at all.
Resistance by swapping the lipid out
Mutants of the alkali-loving bacterium Bacillus firmus selected for resistance had sharply reduced ordinary phosphatidylethanolamine in their membranes, as earlier Bacillus subtilis mutants had. These strains carried substantial amounts of the plasmalogen form of the same lipid instead, an unusual component for a bacterium that needs oxygen, and traces of it were confirmed in the parent strain too. Several other lipid changes came with resistance, and none of them stopped the bacteria growing in alkaline conditions.
The structure, corrected
The lanthionine-containing antibiotic PA48009, isolated from a Streptoverticillium culture, was shown to be duramycin. Edman degradation and two-dimensional nuclear magnetic resonance together established a structure that required revising the one in the existing literature. The corrected molecule differs from the related lantibiotic cinnamycin, also called Ro 09-0198 or lanthiopeptin, only by a lysine in place of an arginine at position two.
How the bacterium builds it
Sequencing Streptomyces cinnamoneus identified the gene cluster that makes duramycin, and expressing those genes in Escherichia coli produced the peptide, along with the natural variant duramycin C. The paper spells out the molecule's unusual parts: one lanthionine and two methyllanthionine bridges, a lysinoalanine bridge joining the amino group of lysine 19 to serine 6, and a hydroxylated aspartate at position 15, each needed for binding phosphatidylethanolamine. Mutating the precursor peptide showed that a single glycine next to the aspartate is required by the enzyme that adds the hydroxyl. Being able to make the peptide in a laboratory bacterium opens the way to engineered versions.
A check for heart rhythm risk
Dogs in toxicology testing had shown extra ventricular beats, so the peptide was tested on the heart's voltage-gated channels in native cells and in an expression system using whole-cell patch clamp. Between 1 nanomolar and 0.1 micromolar nothing happened to hERG potassium, sodium or calcium currents. At 0.3 micromolar and above every current shrank and sodium channel inactivation slowed, and above about 3 micromolar a leak current appeared, consistent with pores forming. The authors attribute all of it to altered membrane properties rather than to any interaction with the channel proteins, and note that inhaled dosing leaves plasma concentrations below 0.5 nanomolar, a wide margin.
Killing tumour cells in culture
Duramycin labelled phosphatidylethanolamine on the surface of pancreatic tumour cells by flow cytometry, with more labelling on apoptotic cells and more still on necrotic ones. Cultured with the peptide, cells became progressively apoptotic and then necrotic as the concentration rose, and proliferation fell steadily between 0.125 and 12.5 micromolar. Tissue factor on the cell surface, which drives clotting, also fell. Electron microscopy showed fragile cells. The authors read the anti-proliferative and anticoagulant effects as consequences of damaging the membrane rather than of any signalling.
Calcium release across fifteen cancer cell lines
The peptide detected surface phosphatidylethanolamine on all fifteen cancer lines screened, in proportion to the concentration used, and the higher concentrations killed the cells by necrosis. It also released calcium inside the cells in a way that depended on both concentration and time. Live confocal imaging of a pancreatic line showed a dye that normally cannot enter cells seeping in over time, alongside changes in cell shape. The calcium release is consistent with the airway work from twenty years earlier and with a membrane that has stopped holding its contents in.
Blocking virus entry by covering a lipid
This paper showed that phosphatidylethanolamine, not just phosphatidylserine, is recognised by the receptors some enveloped viruses use to get into cells, and that the lipid sits in the envelopes of flaviviruses and filoviruses. Duramycin blocked entry of West Nile, dengue and Ebola viruses, and did so specifically: it stopped infection routed through the TIM1 receptor but not through another receptor, by preventing the virus attaching to TIM1 in the first place. The experiments reported were in cells: a demonstration of how the virus gets in, not a test of a treatment.
The same block in placental cells and Zika virus
Primary cells and tissue explants from human placenta of different gestational ages were infected with two strains of Zika virus. The virus grew in several cell types that carry the entry cofactors Axl, Tyro3 or TIM1, with the highest titres in amniotic epithelial cells from mid-gestation placentas. Duramycin, used here because it binds phosphatidylethanolamine in viral envelopes and so blocks TIM1 binding, reduced infection in both the isolated cells and the explants. The authors read the result as evidence for a route of mother-to-fetus transmission worth targeting, not as a candidate treatment.
A recent review of the whole molecule
A 2025 review of duramycin covers its chemistry, how the bacterium assembles it, the role of the lanthionine and methyllanthionine bridges, and the membrane-disrupting mechanism that follows from binding phosphatidylethanolamine. It summarises the clinical history as far as phase 2 in cystic fibrosis, surveys the antiviral work, and discusses the practical obstacles: manufacturing, resistance and delivery. It also covers the uses that have outlasted the drug programme, in cancer research, diagnostics and as a probe for studying membranes.
Where it sat among cystic fibrosis treatments
A review of ways to rehydrate airway mucus in cystic fibrosis sets out the problem: less chloride leaving the cell means less water, a thinner liquid layer around the cilia, worse mucus clearance and plugging. It groups the options into direct osmotic agents, CFTR modulators and drugs aimed at other ion channels, and lists this peptide among the emerging agents in the third group, described as raising calcium inside the cell. At the time of writing only hypertonic saline and the CFTR potentiator ivacaftor were in clinical use for the purpose.
Dosing Data
Every amount below was given inside a clinical trial, nebulised or run across the lining of the nose. There is no approved product, no approved dose, and the largest trial of these amounts found no benefit.
Educational information, not medical advice. Each dose above is tagged with its source: an approved label, a published human study, animal data, or amounts reported by users. None is a recommendation for you. An unapproved compound has no established safe or effective human dose, and products sold for “research use only” are not made or tested for people. Talk to a doctor before acting on anything on this site, including before you start, stop or change any medicine or dose. Full medical disclaimer.
What a Buyer Needs to Know
What is sold, how it is mixed, stored and taken, and what is known about its safety, quality and legal status. Each part names its source. Where we have none, it says unknown.
What is sold
Unknown: we hold no label and no published test that says what forms or vial sizes Lancovutide is sold in. A vial's own label is a seller's claim, not a source.
Mixing a vial: a worked example
No worked example: none of the doses on this page is a fixed amount in mg or mcg injected under the skin or into a muscle (the routes given are: inhaled (nebulised)). There is no home-mixing step to show. The reconstitution calculator does the arithmetic for any vial.
Source: the route and amount of each dose row in Dosing Data below.
Storage before and after mixing
Unknown: no label or published stability study on file says how to store Lancovutide, before or after mixing. The mixing guide sets out the general rules, with their sources: keep a mixed vial in the fridge, and use it promptly, as the bacteriostatic water label says of any drug dissolved in it. The 28 days often quoted is the limit for an opened multiple-dose vial from a manufacturer, an outer limit set for sterility, not a time a mixed solution has been shown to keep. Nobody has published how long Lancovutide stays intact once mixed.
How it is taken
As it was given in human studies: Inhaled (nebulised) (Once a day, every other day, or twice a week (three arms); Study: the 161-patient phase 2 trial).
For injection technique, sites and needle disposal, see the mixing guide.
Source: Used in human trials: the route and frequency of each row in Dosing Data below.
What to expect, and when
How long it stays in the body: a half-life of about 5 days in bronchial epithelial cells and 25 to 91 days in lavage cells after one inhaled dose. After about five half-lives almost none is left.
How long the doses were given: Study: the 161-patient phase 2 trial: 8 weeks; Study: five-day rising-dose phase 2: 5 days; Study: single-dose pharmacokinetics in healthy men: Single dose.
When effects appear: unknown; no source on this page gives a time to effect for Lancovutide. Results reported in the studies are under Published Research.
Source: half-life: PMID 18500510; Used in human trials, the duration of each row in Dosing Data below.
Side effects, and when to stop or get help
From the Side Effects section: In the 161-patient trial, inhalation was judged safe overall, but adverse events, especially respiratory ones, were more frequent on the drug than on placebo (PMID 32888826); One of 24 patients in the five-day trial had a sharp transient fall in FEV1 after inhaling, which recovered without treatment; another had passing numbness of the throat while inhaling (PMID 17494794); No visible nasal irritation, no rise in lavage markers of damage and no change in lung function after nasal superfusion in eight people (PMID 14718433); No inflammatory response in the lung after a single inhaled dose in six healthy men, measured as fourteen cytokines in lavage fluid (PMID 18500510); Undetectable in plasma after inhalation in both the volunteer study and the highest-dose trial group, which limits the scope for effects outside the lung (PMIDs 18500510, 17494794); Extra ventricular beats were seen in dogs during toxicology testing; cell work found no effect on cardiac channels below 0.3 micromolar and attributed the higher-concentration effects to membrane disturbance, with inhaled plasma levels far below that (PMID 18176799). Full list and cautions ↓
When to stop or get help: unknown; no label or trial on file sets rules for stopping Lancovutide. Treat a severe or unexpected reaction as a reason to stop and see a doctor.
Source: the Side Effects section below (“From the human studies above”).
Interactions
Unknown: a PubMed search for human interaction studies of Lancovutide (reviewed 2026-11-04) found none. Unknown is not the same as safe to combine.
Every peptide's record, with its source: the interaction matrix.
Checking what you bought
Unknown: no published independent test of Lancovutide products is in our lab-results database yet, so how products sold under this name measure up is not known.
To read a certificate of analysis, paste it into the COA decoder; it checks the measured mass against Lancovutide's expected mass, 2,013.3 Da, from this entry's molecular data. Trust & Verification explains what independent testing can and cannot show.
Legal status
US: Not FDA Approved (Not approved anywhere). Sport: Prohibited (S0 catch-all).
Country by country ↓ · Regulatory tracker
Source: this entry's approval status and the WADA Prohibited List, as in Legal Status below.
Side Effects & Contraindications
Reported Side Effects
From the human studies above. Three of the four were small, and only the 161-patient trial was large enough to compare rates of anything.
Contraindications & Cautions
There is no label and so no official contraindications. These cautions follow from what the studies show.
Legal Status
Lancovutide is an investigational drug with an EU orphan designation from 2002 and no marketing approval anywhere.
Frequently Asked Questions
?What is lancovutide?
A 19-amino-acid peptide made by a Streptomyces bacterium, known in the laboratory as duramycin. Its rings of sulfur-bridged amino acids put it in the lantibiotic family, alongside nisin. It binds a membrane lipid called phosphatidylethanolamine, and that binding is behind everything it does.
?Why was it tried in cystic fibrosis?
Because it makes airway cells secrete chloride without using CFTR, the channel that cystic fibrosis mutations break. A drug that works around CFTR rather than fixing it would in principle help patients with any mutation, including those no modulator drug reaches.
?Did it work?
No. A 24-patient trial over five days found better FEV1 at the highest dose, which was enough to justify a real test. That test enrolled 161 patients for eight weeks and found no difference from saline in lung function, quality of life, exacerbations or extra treatment needed. No further trial has been registered.
?Is it the same thing as the duramycin used in imaging research?
The peptide is the same molecule, but the imaging agents are not the same product. Those are duramycin chemically joined to a chelator and loaded with technetium-99m, gallium-68 or fluorine-18, and they are injected into a vein to mark dying cells rather than inhaled to treat anything. Findings about them are listed on this page under References, not as studies of this drug.
?Is it an antibiotic?
It kills gram-positive bacteria whose membranes contain phosphatidylethanolamine, and that is how it was first found. It was never developed as an antibiotic for people, and bacteria resist it simply by changing that lipid.
?Can I buy it?
Not as a medicine. It has never been approved or marketed anywhere, and the only human doses were given inside trials that ended more than fifteen years ago. Research-grade duramycin is sold as a laboratory reagent for staining membranes, which is not a medicine and is not what this page is about.
References
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- [clinical-trial] Grasemann H, et al. "Inhalation of Moli1901 in patients with cystic fibrosis." Chest, 2007;131(5):1461-6. PMID: 17494794.
- [clinical-trial] Steiner I, et al. "Pulmonary pharmacokinetics and safety of nebulized duramycin in healthy male volunteers." Naunyn Schmiedebergs Arch Pharmacol, 2008;378(3):323-33. PMID: 18500510.
- [clinical-trial] Eber E, et al. "Aerosolized lancovutide in adolescents (≥12 years) and adults with cystic fibrosis - a randomized trial." J Cyst Fibros, 2021;20(1):61-67. PMID: 32888826.
- [pubmed] McNulty MJ, et al. "Pharmacokinetics and tissue distribution of the nonadecapeptide Moli1901 in rats and mice." Xenobiotica, 2003;33(2):197-210. PMID: 12623761.
- [pubmed] Rickert DE, et al. "Determination of the tissue distribution and excretion by accelerator mass spectrometry of the nonadecapeptide 14C-Moli1901 in beagle dogs after intratracheal instillation." Chem Biol Interact, 2005;155(1-2):55-61. PMID: 15893299.
- [pubmed] Cloutier MM, et al. "Duramycin enhances chloride secretion in airway epithelium." Am J Physiol, 1990;259(3 Pt 1):C450-4. PMID: 2169195.
- [pubmed] Roberts M, et al. "Stimulation of sodium transport by duramycin in cultured human colonic epithelia." J Pharmacol Exp Ther, 1991;259(3):1050-8. PMID: 1762061.
- [pubmed] Cloutier MM, et al. "Duramycin increases intracellular calcium in airway epithelium." Membr Biochem, 1993;10(2):107-18. PMID: 8361390.
- [pubmed] Oliynyk I, et al. "Effect of duramycin on chloride transport and intracellular calcium concentration in cystic fibrosis and non-cystic fibrosis epithelia." APMIS, 2010;118(12):982-90. PMID: 21091780.
- [pubmed] Sheth TR, et al. "Ion channel formation by duramycin." Biochim Biophys Acta, 1992;1107(1):179-85. PMID: 1377492.
- [pubmed] Iwamoto K, et al. "Curvature-dependent recognition of ethanolamine phospholipids by duramycin and cinnamycin." Biophys J, 2007;93(5):1608-19. PMID: 17483159.
- [pubmed] Hasim S, et al. "Elucidating Duramycin's Bacterial Selectivity and Mode of Action on the Bacterial Cell Envelope." Front Microbiol, 2018;9:219. PMID: 29491859.
- [pubmed] Märki F, et al. "Mode of action of the lanthionine-containing peptide antibiotics duramycin, duramycin B and C, and cinnamycin as indirect inhibitors of phospholipase A2." Biochem Pharmacol, 1991;42(10):2027-35. PMID: 1741778.
- [pubmed] Yates KR, et al. "Duramycin exhibits antiproliferative properties and induces apoptosis in tumour cells." Blood Coagul Fibrinolysis, 2012;23(5):396-401. PMID: 22543977.
- [pubmed] Broughton LJ, et al. "Duramycin-induced calcium release in cancer cells." Anticancer Drugs, 2016;27(3):173-82. PMID: 26512767.
- [pubmed] Richard AS, et al. "Virion-associated phosphatidylethanolamine promotes TIM1-mediated infection by Ebola, dengue, and West Nile viruses." Proc Natl Acad Sci U S A, 2015;112(47):14682-7. PMID: 26575624.
- [pubmed] Tabata T, et al. "Zika Virus Targets Different Primary Human Placental Cells, Suggesting Two Routes for Vertical Transmission." Cell Host Microbe, 2016;20(2):155-66. PMID: 27443522.
- [pubmed] Huo L, et al. "Insights into the Biosynthesis of Duramycin." Appl Environ Microbiol, 2017;83(3). PMID: 27864176.
- [pubmed] Hayashi F, et al. "The structure of PA48009: the revised structure of duramycin." J Antibiot (Tokyo), 1990;43(11):1421-30. PMID: 2272918.
- [pubmed] Zebedin E, et al. "Effects of duramycin on cardiac voltage-gated ion channels." Naunyn Schmiedebergs Arch Pharmacol, 2008;377(1):87-100. PMID: 18176799.
- [pubmed] Navarro J et al. "Interaction of duramycin with artificial and natural membranes." Biochemistry, 1985;24(17):4645-50. PMID: 2933071.
- [pubmed] Clejan S, et al. "Mutation of Bacillus firmus OF4 to duramycin resistance results in substantial replacement of membrane lipid phosphatidylethanolamine by its plasmalogen form." J Bacteriol, 1989;171(3):1744-6. PMID: 2921248.
- [review] Yuan M, et al. "Duramycin: Exploring the therapeutic frontier of a unique lantibiotic." Peptides, 2025;193:171447. PMID: 41077020.
- [review] Tildy BE, et al. "Therapeutic options for hydrating airway mucus in cystic fibrosis." Pharmacology, 2015;95(3-4):117-32. PMID: 25823699.
- [pubmed] Zhao M, et al. "99mTc-labeled duramycin as a novel phosphatidylethanolamine-binding molecular probe." J Nucl Med, 2008;49(8):1345-52. PMID: 18632826.
- [pubmed] Metelerkamp Cappenberg T, et al. "First-in-human study of a novel cell death tracer [(99m)Tc]Tc-Duramycin: safety, biodistribution and radiation dosimetry in healthy volunteers." EJNMMI Radiopharm Chem, 2023;8(1):20. PMID: 37646865.
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- [pubmed] Fredenhagen A, et al. "Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin." J Antibiot (Tokyo), 1990;43(11):1403-12. PMID: 2125590.
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- [pubmed] Iliasov D, et al. "Discovery of Coerumycin, a Cinnamycin-like Lantibiotic from Actinomadura coerulea TMS085." Antibiotics (Basel), 2026;15(1). PMID: 41594142.
- [pubmed] Sokolove PM, et al. "Duramycin effects on the structure and function of heart mitochondria. I. Structural alterations and changes in membrane permeability." Biochim Biophys Acta, 1989;983(1):15-22. PMID: 2758048.
- [pubmed] Dunkley EA Jr, et al. "Large decreases in membrane phosphatidylethanolamine and diphosphatidylglycerol upon mutation to duramycin resistance do not change the protonophore resistance of Bacillus subtilis." Biochim Biophys Acta, 1988;943(1):13-8. PMID: 3135835.
- [pubmed] Rzeźnicka II, et al. "Duramycin-induced destabilization of a phosphatidylethanolamine monolayer at the air-water interface observed by vibrational sum-frequency generation spectroscopy." Langmuir, 2010;26(20):16055-62. PMID: 20873825.
- [other] ChEMBL CHEMBL2108327 (LANCOVUTIDE; synonyms Duramycin, Lancovutida, Leucopeptin, MOLI-1901, Moli1901), molecule type Protein, maximum phase 2; read November 4, 2026. https://www.ebi.ac.uk/chembl/compound_report_card/CHEMBL2108327/
- [other] UniProt P36504, lantibiotic duramycin (antibiotic PA48009, leucopeptin) from Streptomyces griseoverticillatus, mature sequence CKQSCSFGPFTFVCDGNTK, 19 residues; read November 4, 2026. https://www.uniprot.org/uniprotkb/P36504/entry
- [fda] US FDA, Drugs@FDA and drug label endpoints (openFDA), searched November 4, 2026: no record for lancovutide, duramycin or Moli1901. https://api.fda.gov/drug/drugsfda.json
- [registry] European Medicines Agency, orphan designation EU/3/02/120, duramycin for the treatment of cystic fibrosis, granted November 13, 2002 to a German sponsor and transferred to an Austrian company in December 2004; status Positive, record last updated February 4, 2022. The page also records that US orphan drug status for cystic fibrosis was granted on December 11, 1997. Read November 4, 2026. https://www.ema.europa.eu/en/medicines/human/orphan-designations/eu-3-02-120
- [clinicaltrials] ClinicalTrials.gov, searched November 4, 2026: NCT00671736, "Lancovutide (Moli1901) Inhalation Solution Study in Adolescents and Adults With Cystic Fibrosis", phase 2, completed July 2009, 160 planned participants, no results posted. No other registered study of this peptide. https://clinicaltrials.gov/study/NCT00671736
Sources & Citations
Every study on this page was read from its PubMed record on November 4, 2026. The trial registration comes from ClinicalTrials.gov, the sequence and ring structure from UniProt and the biosynthesis paper, and the regulatory status from Drugs@FDA, openFDA and the EU orphan register, read the same day. Grey Peptides sells nothing and links to no vendor.
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