pe
pep-10981 v1 CC-BY-SA-4.0

Lanreotide: Somatuline, treatment for acromegaly and neuroendocrine tumors

A synthetic hormone shot given monthly that slows excess growth hormone and shrinks certain hormone-releasing tumors; FDA-approved drug.

statuscomputed targetSSTR2 length9 aa refs3
status 2 / 5
prediction metrics boltz-2 2.2.1
ipTM0.984
pTM0.969
avg pLDDT75.5
ranking score0.800
STRUCTURE · PEP-10981 × SSTR2
ranking0.800
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 2.2.1 · mmCIF ↓ download
sequence9 aa
159
XCYFWKVCT
in the news 4 articles
overview readme

What this is

Lanreotide (brand names Somatuline® Depot and Somatuline Autogel®, made by Ipsen) is a monthly or longer-interval injection used to treat acromegaly (a condition of excess growth hormone), certain types of neuroendocrine tumors, and carcinoid syndrome. It is a synthetic peptide that mimics somatostatin — a natural hormone that puts the brakes on several secretory processes in the body. Lanreotide is FDA-approved and EMA-approved for these indications. It is also known by its developmental code BIM-23014. The stored sequence XCYFWKVCT is a standard-letter approximation of the active cyclic molecule; the true structure contains a D-β-naphthylalanine residue at position 1, a D-tryptophan at position 4, a disulfide bridge between cysteines 2 and 7 forming the ring, and a C-terminal amide — none of which are visible in the raw sequence.

History

Lanreotide was developed by Ipsen during the 1980s–90s as a longer-acting alternative to octreotide (developed by Sandoz/Novartis), using β-2-naphthylalanine as a novel pharmacophore modification. An early formulation (BIM23014) had a half-life of approximately 90 minutes (Gomes-Porras and colleagues, International Journal of Molecular Sciences 2020). A sustained-release formulation followed, and then the self-forming Autogel — a supersaturated aqueous gel in which the molecule self-assembles into nanotube structures — extended dosing intervals to monthly or beyond when delivered by deep subcutaneous injection. European approval for acromegaly came in the early 1990s; the FDA approved lanreotide for acromegaly in 2007. The CLARINET Phase 3 trial, published in the New England Journal of Medicine in 2014 (Caplin and colleagues), established lanreotide for unresectable gastroenteropancreatic NETs, demonstrating that it reduced the risk of tumor progression or death by 53% compared with placebo (HR 0.47) — the first large prospective randomized trial to show anti-tumor disease stabilization with a somatostatin analog. FDA approval for GEP-NETs followed in 2014, and for carcinoid syndrome in 2017.

What it does

Lanreotide binds primarily to somatostatin receptor type 2 (SSTR2) and to a lesser extent SSTR5. These receptors are found on pituitary growth-hormone-secreting cells, on enterochromaffin and neuroendocrine tumor cells, and in other tissues. By activating SSTR2, lanreotide suppresses the release of growth hormone (GH) — which in acromegaly reduces elevated IGF-1 levels and reverses the tissue overgrowth, cardiovascular strain, and metabolic effects of the disease. In neuroendocrine tumors, SSTR2 activation slows cell division and reduces blood-vessel formation within the tumor, stabilizing disease without typically causing regression. In carcinoid syndrome, it suppresses release of serotonin and other mediators from enterochromaffin cells, reducing flushing and diarrhea. The Autogel depot formulation is designed to avoid the high concentration peaks associated with other injectable formulations, providing steadier exposure across the dosing interval.

Evidence

  • Human: The CLARINET Phase 3 trial (Caplin and colleagues, NEJM 2014) randomized 204 patients with non-functioning well-differentiated gastroenteropancreatic NETs (grade 1 or 2, Ki-67 <10%) to lanreotide 120 mg every 28 days versus placebo; median progression-free survival was not reached in the lanreotide arm versus 18.0 months on placebo (HR 0.47, 95% CI 0.30–0.73, p=0.0002), a 53% reduction in the risk of progression or death. In acromegaly, a meta-analysis of long-acting somatostatin analog therapy reported GH normalization below 2.5 ng/mL in 57–67% of patients on lanreotide and IGF-1 normalization in 60–65% (Freda and colleagues, Journal of Clinical Endocrinology & Metabolism 2005). The ELECT Phase 3 trial (Vinik and colleagues, Endocrine Practice 2016) established carcinoid syndrome symptom control by showing that lanreotide 120 mg every 4 weeks significantly reduced the need for rescue short-acting octreotide compared with placebo over 16 weeks. More recent reviews continue to position lanreotide alongside ¹⁷⁷Lu-DOTATATE in the SSTR2-targeted treatment sequence for pancreatic NETs (Karimi and colleagues, npj Precision Oncology 2025).
  • Animal: In SSTR2-positive NET xenograft models, lanreotide reduces tumor growth with confirmed anti-angiogenic effects (VEGF reduction). In a rat prostate tumor model, lanreotide was as effective as castration (Gomes-Porras and colleagues, International Journal of Molecular Sciences 2020), and therapeutic benefit was also observed in the hormone-resistance phase.
  • In vitro: Mechanistic studies confirm SSTR2/5 binding and downstream suppression of cyclic AMP, calcium channel activity, and proliferative signaling.

Known effects

  • GH/IGF-1 suppression in acromegaly — FDA-approved (normalization in majority of patients)
  • GEP-NET disease stabilization — FDA-approved; 53% reduction in progression-or-death risk in CLARINET
  • Carcinoid syndrome symptom control — FDA-approved (ELECT trial)
  • SSTR2/5 agonism → anti-proliferative cell-cycle effects — established in clinical and preclinical data
  • Flexible dosing interval (monthly to trimonthly) — in patients with stable disease on standard dosing

Safety signals

The safety profile of lanreotide closely resembles that of octreotide, as expected from the shared SSTR2/5 mechanism. Gallstone formation (cholelithiasis) is the most prominent long-term signal: a comparative pharmacovigilance analysis of the FDA Adverse Event Reporting System (Scientific Reports 2025) found a strong disproportionality signal for cholelithiasis with lanreotide (Reporting Odds Ratio 12.03, 95% CI excluding 1), and long-term clinical follow-up describes cholelithiasis in roughly 20–33% of lanreotide-treated patients (Gomes-Porras and colleagues, International Journal of Molecular Sciences 2020). Gastrointestinal symptoms — diarrhea, abdominal pain, loose stools, nausea — are common and were more frequently associated with lanreotide than with octreotide in the same FAERS analysis. Injection-site reactions occur with the deep subcutaneous Autogel formulation. Bradycardia and mild hyperglycemia (somatostatin suppresses insulin secretion) have also been reported. The same FAERS analysis found lanreotide carries comparatively lower cardiovascular and neoplastic safety signals than octreotide, and long-term tolerability over several years of treatment is generally considered acceptable.

Regulatory status

  • US: Prescription-only. FDA-approved for acromegaly (Somatuline Depot® 60/90/120 mg SC, 2007), unresectable well-differentiated GEP-NETs (2014), and carcinoid syndrome (2017). Three separate approved indications.
  • EU: EMA-approved as Somatuline Autogel® for acromegaly and NETs.
  • WADA: Somatostatin analogs are not listed on the WADA Prohibited List for general sport; their use in medical indications does not require a Therapeutic Use Exemption.

Related peptides

  • Octreotide (/card/pep-10808) — the first marketed SSTR2/5 analog; available as octreotide LAR for monthly injection; same mechanism and primary indications.
  • Somatostatin-14 (/card/pep-10641) — the endogenous parent hormone; short half-life (1–3 min) makes it unsuitable for chronic use, which drove the development of lanreotide and octreotide.
  • Somatostatin-28 (/card/pep-10642) — the extended endogenous form with a longer sequence; also acts at SSTR2 but with different receptor subtype distribution.
  • Pasireotide — pan-SSTR agonist (SSTR1/2/3/5); approved for Cushing's disease; broader receptor profile than lanreotide with distinct metabolic side-effect profile.

Mechanism

Lanreotide's full chemical name reflects a ring structure: [D-β-2-Nal¹]-Cys²-Tyr³-D-Trp⁴-Lys⁵-Val⁶-Cys⁷-Thr⁸-NH₂, with a disulfide bridge between Cys2 and Cys7. The β-2-naphthylalanine at position 1 provides hydrophobic stacking with SSTR2 and SSTR5 transmembrane helices, conferring nanomolar affinity (SSTR2 IC₅₀ ~0.5 nM). Upon SSTR2 binding, the receptor couples to Gi/o proteins, reducing intracellular cyclic AMP (cAMP), closing voltage-gated calcium channels, and blocking secretory vesicle exocytosis — the mechanism by which GH, serotonin, and other hormones are suppressed. The anti-proliferative effect operates through a separate pathway: SSTR2 activates protein tyrosine phosphatases (SHP1/PTP-η), which attenuate Ras/MAPK signaling and induce G1-phase cell cycle arrest by reducing CDK2/4 activity. The Autogel formulation disperses the peptide in a polysorbate/carmellose microsphere matrix; once injected deep subcutaneously, slow aqueous dissolution of the depot produces a flat pharmacokinetic profile across the monthly dosing interval, avoiding the concentration peaks associated with bolus injection.

Open questions

  • Whether the progression-free survival benefit demonstrated in CLARINET translates to an overall survival benefit — extended follow-up data show a trend but no definitive OS signal.
  • Whether lanreotide provides anti-tumor benefit in higher-grade (Ki-67 > 10%) G2/G3 NETs beyond hormonal symptom control.
  • The role of lanreotide in SSTR2-negative tumors that emerge after progression, and optimal sequencing with mTOR inhibitors (everolimus) or peptide receptor radionuclide therapy (PRRT, e.g., ¹⁷⁷Lu-DOTATATE).
Hypotheses5 directions▾ collapse

Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.

openupdated 2026-06-05

Does long-term lanreotide treatment reliably prevent growth of small pancreatic tumors in people with a hereditary tumor syndrome, and does this protection last beyond two years?

People with MEN1 syndrome develop multiple pancreatic tumors across their lifetime and often face repeated surgeries. If lanreotide can hold small tumors stable for many years, some patients might avoid or substantially delay operations, improving quality of life considerably.

The hypothesis
Lanreotide's sustained sstr2 agonism could suppress tumor growth in MEN1-related pancreatic neuroendocrine tumors smaller than 20 mm through a direct antiproliferative mechanism beyond secretion inhibition, and continued therapy beyond 24 months extends progression-free survival in a size-dependent manner.
Why it’s plausible
A prospective study in MEN1-related NETs under 20 mm diameter reported significantly higher median progression-free survival with lanreotide 120 mg over 24-84 months. Somatostatin receptor subtype 2 is coupled to multiple antiproliferative signaling cascades (Gi/o suppression of cAMP, phosphotyrosine phosphatase activation, and induction of apoptosis) that are separable from the secretory inhibition effect. Whether the long-term tumor control is maintained or eroded beyond 24 months, and whether it varies with initial tumor size within the less-than-20-mm range, is not established.
Why it matters
MEN1 patients face lifelong tumor surveillance; a non-surgical antiproliferative option that is durable and size-stratifiable would substantially change the management algorithm for small pancreatic NETs, potentially deferring or avoiding surgery.
Plausibility.75
Novelty.50
Impact.75
Basis · grounding2 papers
[1]
paper
Prospective study: lanreotide 120 mg every 28 days for 24-84 months in 23 MEN1 patients with NETs under 20 mm showed significantly higher median progression-free survival.
doi: 10.3390/ijms21051682
[2]
paper
Lanreotide administered subcutaneously at 120 mg every 28 days; dose individualization guidelines absent, suggesting unexplored optimization space.
doi: 10.1159/000548257
openupdated 2026-06-05

Is lanreotide's exceptional binding strength mostly due to its pre-shaped ring structure rather than the usual flexible lock-and-key process?

If rigidity is the key, drug designers could copy that ring-constraining trick to make other peptide drugs bind more tightly and specifically, potentially reducing side effects and enabling lower doses in future somatostatin-targeting medicines.

The hypothesis
Lanreotide's exceptionally high structure-prediction confidence (ipTM 0.984) at sstr2 reflects a rigid, pre-organized binding conformation imposed by its disulfide-cyclized backbone and D-amino acid substitutions, and this conformational pre-organization is the primary driver of its subnanomolar sstr2 affinity rather than flexible induced-fit contacts.
Why it’s plausible
The stored sequence XCYFWKVCT represents a cyclic peptide constrained by a disulfide bridge between positions 2 and 7, with a D-beta-naphthylalanine at position 1 and D-tryptophan at position 4. Such conformational rigidity is known to reduce entropic cost of binding. An ipTM of 0.984 is among the highest plausible for a small cyclic peptide, suggesting the predicted interface is highly ordered. If pre-organization dominates affinity, even small changes outside the pharmacophore triad (Phe/Trp/Lys core) should have minimal effect on potency, a falsifiable distinction from induced-fit models.
Why it matters
Understanding whether lanreotide affinity is entropy-driven (pre-organization) or enthalpy-driven (induced-fit) has direct implications for designing next-generation sstr2 ligands: pre-organization favors cyclization strategies, while induced-fit favors flexible linker optimization.
Plausibility.80
Novelty.50
Impact.65
Basis · grounding3 computed/notes
[1]
structureBoltz-2 complex ipTM=0.984, the highest in this batch, consistent with a rigid, well-defined binding pose.
[2]
noteLanreotide contains D-beta-naphthylalanine at position 1, D-tryptophan at position 4, disulfide bridge between Cys2 and Cys7, and C-terminal amide, all of which enforce a rigid cyclic conformation.
[3]
sourceAmino acid substitutions on critical portions suggest a structurally related receptor binding mode; pharmacophore core is conserved.
openupdated 2026-06-05

Does the bulkier chemical group at position 1 in lanreotide make it grab onto one receptor subtype more tightly than octreotide does, creating different patient response patterns?

Many acromegaly patients do not fully respond to either drug. If this structural difference predicts who benefits from which agent, doctors could match patients to the right medicine from the start, saving months of ineffective treatment.

The hypothesis
Lanreotide's D-beta-naphthylalanine at position 1 confers preferential sstr2 selectivity over sstr5 compared to octreotide, which uses a standard Phe at the equivalent position, and this difference underlies distinct clinical efficacy profiles at equivalent doses across acromegaly subtypes.
Why it’s plausible
Octreotide and lanreotide both target sstr2/sstr5 but have different receptor selectivity profiles, likely attributable to the bulkier D-beta-naphthylalanine versus D-Phe in octreotide. The clinical literature notes differential response rates among acromegaly subtypes between the two agents. If the naphthylalanine residue specifically alters the depth or orientation of insertion into the sstr2 orthosteric pocket relative to sstr5, this could explain why some patients respond better to one agent than the other.
Why it matters
A mechanistic pharmacophore explanation for lanreotide vs. octreotide selectivity differences would allow rational design of sstr2-pure agonists (minimizing sstr5-mediated GH-independent effects) or sstr2/5 dual agents optimized for specific tumor genotypes.
Plausibility.70
Novelty.55
Impact.70
Basis · grounding1 paper · 2 computed/notes
[1]
noteD-beta-naphthylalanine at position 1 is described as a novel pharmacophore modification distinguishing lanreotide from octreotide.
[2]
paper
Octreotide LAR secondary therapy data across 612 subjects shows differential biochemical responses; receptor subtype selectivity is a plausible source of variance.
doi: 10.1210/jc.2005-0260
[3]
sourceAmino acid substitutions on critical portions indicate receptor binding is sensitive to pharmacophore structure.
openupdated 2026-06-05

Does the amide group capping the tail of lanreotide make a specific contact with the somatostatin-2 receptor that is absent at the somatostatin-5 receptor?

If this end-cap is responsible for receptor selectivity, chemists could tune it to create drugs that hit only the desired receptor, reducing off-target effects and potentially improving efficacy in specific tumor types that express one subtype more than the other.

The hypothesis
The C-terminal amide of lanreotide is necessary for maintaining the disulfide-bridged ring geometry required for sstr2 recognition, and its removal or substitution to a free carboxylate would disproportionately reduce sstr2 affinity relative to sstr5, revealing a subtype-specific C-terminal contact point.
Why it’s plausible
The bioactive ring of lanreotide is closed by a disulfide bond between Cys2 and Cys7, with the C-terminal amide contributing to the overall charge distribution and tail conformation. Amide versus carboxylate at the C-terminus alters local dipole and hydrogen-bonding capacity. If sstr2 and sstr5 differ in the geometry of their extracellular loops contacting the C-terminal region, a C-terminal amide-to-acid substitution could differentially erode sstr2 versus sstr5 binding. The lanreotide core pharmacophore data in the BMC literature supports sensitivity of the ring to substitution effects.
Why it matters
Identifying a C-terminal subtype specificity contact would provide a new design handle for engineering sstr2-selective or sstr5-selective analogues without altering the central Phe-Trp-Lys pharmacophore that dominates current SAR efforts.
Plausibility.65
Novelty.65
Impact.65
Basis · grounding3 computed/notes
[1]
noteC-terminal amide is a defined structural feature of lanreotide distinct from a free carboxylate; its role in receptor subtype selectivity has not been characterized.
[2]
sourceAmino acid substitutions on critical portions and plausibility of structurally related receptors indicate the ring is sensitive to structural variation.
[3]
structureipTM 0.984 for the sstr2 complex; if C-terminal contacts contribute to this score, their removal should be detectable as a drop in confidence.
openupdated 2026-06-05

Could the tiny tubes that lanreotide naturally forms in solution be used to package and slowly release other cancer drugs at a tumor site?

If lanreotide can act as its own delivery vehicle, oncologists might one day inject a single preparation that both controls tumor secretion and delivers a targeted cancer-killing agent, without needing to develop an entirely new drug carrier from scratch.

The hypothesis
Lanreotide's self-assembling nanotube formation in aqueous gel could serve as a drug-delivery scaffold for co-encapsulating other sstr2-expressing tumor-targeting payloads, such as radiolabeled somatostatin analogues or cytotoxic agents, achieving local sustained release at injection sites near tumor beds.
Why it’s plausible
The Autogel formulation of lanreotide exploits spontaneous self-assembly into nanotube structures in supersaturated aqueous solution, enabling deep subcutaneous depots with prolonged release. This self-assembly property is intrinsic to the cyclic peptide scaffold and could, in principle, trap or associate with other molecules during formulation. Radiolabeled SSTR-targeting agents such as 212Pb-DOTAMTATE are already in clinical use; a lanreotide nanotube carrier at a peri-tumoral injection site could combine passive depot release with receptor-targeted delivery.
Why it matters
If lanreotide nanotubes can co-encapsulate a cytotoxic or radiopharmaceutical payload, this would transform an approved depot drug into a platform for local-regional tumor therapy without new synthesis of a novel carrier.
Plausibility.45
Novelty.75
Impact.60
Basis · grounding1 paper · 1 computed/note
[1]
noteLanreotide Autogel self-assembles into nanotube structures in supersaturated aqueous solution; this property is intrinsic to the molecule and drives its depot pharmacokinetics.
[2]
paper
212Pb-DOTAMTATE radiolabeled SSTR-targeting agent is in clinical trials for metastatic SSTR-expressing NETs, confirming receptor-targeted radiotherapy is a validated approach.
doi: 10.1038/s41698-025-00938-1
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.9837395548820496 boltz-2
ranking score 0.800366222858429 boltz-2
3-letter notation
X-Cys-Tyr-Phe-Trp-Lys-Val-Cys-Thr
recipeboltz-2 2.2.1
parametervalue
modelboltz-2 2.2.1
weights
hardwarevast_v100_32gb
mlx version
python
random seed1
msa strategycolabfold_local
runtime
predicted by
predicted at2026-05-22
citationbibtex
peptidemodel (2026). Lanreotide: Somatuline, treatment for acromegaly and neuroendocrine tumors (pep-10981, v1). PeptideModel. https://peptidemodel.com/card/pep-10981
@peptide{pep10981,
  sequence = {XCYFWKVCT},
  target   = {sstr2},
  author   = {peptidemodel},
  year     = {2026},
  status   = {computed}
}
clinical trials 124 on ct.gov · 83 on EUCTR · checked 2026-05-22
ct.gov trials 124
with results 34
EUCTR 83
PubMed RCT 54
by phase
1phase 14phase 23phase 32no phase
by status
3completed3terminated1withdrawn3unknown
references 3 papers
[1]
Long-Acting Somatostatin Analog Therapy of Acromegaly: A Meta-Analysis
Freda, Pamela U. et al. The Journal of Clinical Endocrinology & Metabolism 2005
primary
[2]
Somatostatin Analogs in Clinical Practice: A Review
Gomes-Porras, Mariana et al. International Journal of Molecular Sciences 2020
supporting
discussion no comments
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