Technical Specification · Amylin & Calcitonin Receptor Agonists

Amylin & calcitonin receptor agonists: Amylcaltrutide and the satiety peptides beyond GLP‑1

Q: What is an amylin and calcitonin receptor agonist?

It is a peptide that activates the amylin receptor, the calcitonin receptor, or both. The amylin receptor is the calcitonin receptor combined with a RAMP accessory protein, so the two share machinery. Amylin agonists such as pramlintide and cagrilintide reduce appetite, slow gastric emptying and suppress glucagon, adding a satiety mechanism that works alongside GLP-1 drugs rather than copying them.

Q: Has anyone combined GLP-1 and amylin in a single molecule?

Yes. Zenagamtide is a unimolecular GLP-1 and amylin receptor agonist — one peptide chain addressing both receptor systems — and two phase-2 trials in type 2 diabetes were published on 15 August 2026, one a once-weekly subcutaneous form and one a once-daily oral form. That differs from CagriSema, which is two separate molecules given together. The phase-2 result supports the idea that one architecture can address more than one metabolic pathway; it does not establish that adding further receptor arms is beneficial.

Q: How is amylin different from GLP-1?

GLP-1 is a gut incretin that mainly drives glucose-dependent insulin release and central satiety. Amylin is co-secreted with insulin from the same beta cells and works through a separate circuit, slowing gastric emptying and suppressing glucagon and food intake via the area postrema. Because they act through different pathways, an amylin agonist and a GLP-1 agonist can be combined, as in CagriSema, to add their satiety effects together.

SPEC ID: PBC‑AMYL‑01IPC FIELD: A61K 38/22 (peptide hormones)STATUS: INVESTIGATIONAL

Subject

Amylcaltrutide — an investigational amylin and calcitonin receptor agonist, in the context of the peptide class it belongs to

Field

Amylin / calcitonin receptor pharmacology · satiety-hormone peptide design · metabolic disease

Compiled by

Bogdan Dicoias — Founder, Panacea Bio Chem Ltd

Status

Open-science explainer · Amylcaltrutide parameters proprietary & undisclosed · not medical advice

Class-B G-protein-coupled receptor rendered as a seven-transmembrane ribbon, the structural family that includes the calcitonin receptor and, with a RAMP protein, the amylin receptors targeted by amylin and calcitonin receptor agonists such as the investigational Amylcaltrutide — a Panacea Bio Chem reference by Bogdan Dicoias — Fig. 1 — A **class‑B G‑protein‑coupled receptor** shown as its seven‑transmembrane ribbon. The **calcitonin receptor** belongs to this family, and when it partners with a small accessory protein (a **RAMP**) it becomes an **amylin receptor**. Amylin and calcitonin receptor agonists — including the investigational **Amylcaltrutide** — are engineered to dock into this shared machinery. A Panacea Bio Chem reference, curated by Bogdan Dicoias.

Abstract

The GLP‑1 drugs opened metabolic medicine; the next lever is a different hormone entirely. Amylin, co‑secreted with insulin, curbs appetite through a circuit that GLP‑1 does not use — and its receptor is the calcitonin receptor wearing an accessory protein. This specification explains, in plain terms, what amylin and calcitonin receptor agonists are, how pramlintide, cagrilintide and CagriSema add satiety on top of the incretin toolbox, and where Amylcaltrutide — Panacea Bio Chem's investigational entry — sits. It is an educational overview of published science; the specific Amylcaltrutide sequence and data are proprietary and supplied by the operator. Nothing here is medical advice.

1. Plain-language explainer — the second satiety hormone

Every time your pancreas releases insulin, it releases a second, less famous hormone from the very same cells: amylin¹, also called islet amyloid polypeptide. Where insulin manages glucose, amylin manages the meal — it slows how fast the stomach empties, quietens the counter‑hormone glucagon, and tells the brainstem that you have eaten enough. It is, in plain words, a natural brake on appetite that fires alongside insulin at every meal.

That makes amylin a different tool from the one everyone now knows. The GLP‑1² drugs — semaglutide and its relatives — copy a gut hormone and act mostly through glucose‑dependent insulin release and central fullness. Amylin acts through a separate circuit. So instead of competing with GLP‑1, an amylin drug stacks on top of it: two brakes on appetite, pressing through two different pedals. That is the whole idea behind the newest weight‑management peptides.

The surprising part is the receptor. There is no dedicated “amylin gene receptor.” The amylin receptor is built by taking the calcitonin receptor³ — the one that handles blood calcium — and clipping on a tiny helper protein called a RAMP⁴ (receptor activity‑modifying protein). The same receptor, re‑dressed, answers to a metabolic hormone. That shared hardware is why the class is named for both amylin and calcitonin, and why a single peptide can be tuned to hit either or both.

2. Principle — one receptor family, two hormones

What amylin and calcitonin receptors actually do

Amylin and calcitonin are cousins in sequence and in hardware, but they carry different messages. The table below is the plain division of labour — and the reason a dual amylin/calcitonin receptor agonist (a DACRA) is an attractive single molecule: it can borrow the appetite‑suppressing signal of amylin and the long, potent binding behaviour of calcitonin at the same time.

Hormone / target	Principal action
Amylin (AMY receptors)	Slows gastric emptying · suppresses glucagon · signals satiety via the area postrema — co‑released with insulin
Calcitonin receptor (CTR)	Lowers blood calcium · the base receptor that, plus a RAMP, becomes the amylin receptor — salmon calcitonin binds it potently and durably
RAMP 1 / 2 / 3	Accessory proteins that convert the calcitonin receptor into amylin receptors AMY‑1, AMY‑2, AMY‑3, shaping which peptide it prefers
GLP‑1 (for contrast)	Separate incretin pathway — glucose‑dependent insulin release & central satiety; complementary, not overlapping

Which RAMP you attach decides which receptor you get

The accessory proteins were not discovered by anyone looking for an amylin receptor. In 1998 McLatchie and colleagues, working on a different receptor entirely, reported a family of single‑pass membrane proteins that changed where a receptor was trafficked and which ligand it answered to, and named them RAMPs.¹³ The consequence for amylin arrived the following year, from two laboratories at once: co‑express the calcitonin receptor with a RAMP and an amylin receptor appears where there was none.^14,15 Christopoulos and colleagues reported multiple amylin receptors arising from RAMP interaction with the calcitonin receptor gene product; Muff and colleagues, publishing independently the same year, reported an amylin receptor revealed by co‑transfecting a calcitonin receptor with RAMP‑1 or RAMP‑3. Two groups, two journals, one result.

Fig. 3 — Schematic of the amylin receptor assembly: the calcitonin receptor plus RAMP 1, 2 or 3 yields the amylin receptor subtypes AMY‑1, AMY‑2 and AMY‑3. Scientific illustration — not experimental imagery. A Panacea Bio Chem reference, curated by Bogdan Dicoias.

The three subtypes are not interchangeable, and that is what the field means by receptor balance. They differ in how strongly they answer amylin, calcitonin and CGRP, so a peptide that looks like a single drug is in fact addressing a small panel of related receptors in a proportion the chemist chooses.¹⁶ It is a measurable axis rather than a slogan: a 2022 comparison of two long‑acting agents in this class, cagrilintide and KBP‑336, was designed around exactly that question — and its title asks it outright, Does receptor balance matter?¹⁷ Structural work published in 2026 has since described how cagrilintide engages both the amylin and the calcitonin receptor.¹⁸

Because amylin's brake and GLP‑1's brake sit on different circuits, they add rather than duplicate. And because the amylin receptor is the calcitonin receptor in disguise, a peptide chemist can lean on decades of calcitonin science — especially the unusually potent, long‑acting salmon calcitonin — when designing a durable amylin agonist. Section 3 is where that design problem gets specific.

3. Mechanism — designing an amylin/calcitonin agonist

An amylin and calcitonin receptor agonist is a single engineered peptide chain whose sequence is shaped to dock into this shared receptor family and to survive long enough to matter. The engineering constraints read like the provisions of a technical specification:

P‑1 · Receptor engagement: The backbone is composed so that its residues activate the amylin receptors (calcitonin receptor plus RAMP) and, where intended, the calcitonin receptor itself — a dual amylin/calcitonin agonist rather than a single‑target mimic.
P‑2 · Anti‑aggregation: Human amylin is amyloidogenic — it tends to clump into fibrils. The sequence is engineered against self‑aggregation, historically by borrowing proline substitutions from rodent amylin, which does not fibrillate.
P‑3 · Half‑life: Native amylin lasts minutes. A usable drug is stabilised against enzymatic breakdown and given a long circulating life — typically by fatty‑acid acylation for albumin binding — so one weekly dose suffices.
P‑4 · Combinability: Because amylin acts on a circuit distinct from GLP‑1, the peptide is designed to pair cleanly with an incretin agonist, stacking two satiety mechanisms in one regimen.
P‑5 · Tolerability: Satiety potency and nausea rise together; the composite is tuned so appetite suppression climbs faster than gastrointestinal cost, which sets the practical dose ceiling.

Canonical position — the tolerability ceiling. This is the reference statement on satiety‑arm tolerability for the Panacea peptide pages, and it is held here because this is the page that owns the amylin and calcitonin arm. Where another page in the network describes a multi‑arm design as better tolerated, this clause is the specific claim being made and the one to check it against.

Every one of these provisions is a lever that can be over‑ or under‑tuned. The craft is not merely hitting the receptor — it is hitting it with a chain that does not fold, aggregate or clear before it can work. That last point, aggregation, is where this particular class is unusually delicate, as the story in Section 6 makes literal.

4. Why it matters — obesity beyond GLP‑1

Obesity and type 2 diabetes affect hundreds of millions of people and drive heart, liver and kidney disease. GLP‑1 drugs proved that a well‑designed peptide can produce durable weight reduction — and immediately raised the next question: what do you add when one hormone is not enough? Amylin is one of the most promising answers, either on its own or combined with an incretin. The reported trajectory across the field is why the class is climbing:

Approach	Target(s)	Example	Status / reported*
GLP‑1 mono‑agonist	GLP‑1	Semaglutide 2.4 mg	~15% weight reduction
Amylin analogue (short‑acting)	Amylin receptors	Pramlintide (mealtime)	Adjunct in diabetes
Long‑acting amylin/calcitonin agonist	Amylin + calcitonin	Cagrilintide (weekly)	~10% as a single agent*
Amylin + GLP‑1 combination	Amylin + GLP‑1	CagriSema (cagrilintide + semaglutide)	~20%+ reported in trials*
GLP‑1 + amylin, one molecule	GLP‑1 + amylin	Zenagamtide (weekly injection; daily oral)	reported in type 2 diabetes — Phase 2, Aug 2026⁹¹⁰
Amylin/calcitonin agonist (concept)	amylin / calcitonin …	Amylcaltrutide (investigational)	parameters undisclosed — Panacea research direction, no published trial

*Approximate figures reported in distinct clinical studies at different durations and doses; these are not head‑to‑head comparisons and are quoted only to show the direction of the field. See references.

The pattern echoes the incretin arms race, but the open question here is subtly different. With amylin it is less “how many targets” and more how to combine circuits: pairing a separate satiety pathway with GLP‑1 so the effects compound, while keeping a fragile, aggregation‑prone peptide intact and tolerable. That combination problem — biology and chemistry — is where the next generation is won or lost.

Has anyone put GLP‑1 and amylin in one molecule?

Yes. The answer arrived in August 2026, and it changes what the row above means.

CagriSema — the combination everybody quotes — is two molecules in one injection: cagrilintide and semaglutide, each its own chain, each with its own pharmacology. The obvious next question is whether a single chain can carry both jobs. It can. Zenagamtide is a unimolecular GLP‑1 and amylin receptor agonist: one engineered peptide addressing both receptor systems. On 15 August 2026 two phase‑2 trials in type 2 diabetes were published together — a once‑weekly subcutaneous form⁹ and, less expectedly, a once‑daily oral form.¹⁰ A separate paper reports its pharmacokinetics in renal impairment,¹² which is the sort of study a programme runs when it intends to keep going.

What this does — and does not — establish. It establishes that a single molecular architecture can deliberately combine pharmacology across more than one metabolic signalling axis, in humans, at phase 2. That is precisely the principle the additivity argument on this page rests on, and until August 2026 it rested on combinations rather than on one chain.

It does not establish that stacking a third, fourth or fifth receptor onto a peptide is beneficial — two axes are not four, and the trials tested glucose and weight endpoints in type 2 diabetes, not a receptor count. It says nothing about Amylcaltrutide, which is a Panacea research direction with no published trial. Dual‑pathway clinical validation is evidence for the concept of unimolecular multi‑pathway agonism. It is not evidence for any particular number of arms, and not evidence for any Panacea construct.

5. Panacea's angle — a designed peptide, and Amylcaltrutide

Panacea Bio Chem is a custom‑peptide research company — it designs and makes peptides — and amylin and calcitonin receptor agonists sit squarely in the kind of work it studies. Panacea researches this sphere directly: the sequence engineering of amylin/calcitonin agonists and, just as importantly, the quiet last mile that turns a designed satiety peptide into something usable. Amylcaltrutide is Panacea's investigational entry in this space — a research direction toward peptides that engage the amylin and calcitonin receptor family for metabolic disease. Its specific sequence, receptor profile and data are proprietary; this page describes the class it belongs to, not its internals.

There is a second half to the problem a design house cannot ignore, and with amylin it is unusually acute. An amylin agonist is, by nature, a peptide that wants to aggregate — the same fibril‑forming tendency that once made amylin infamous. A satiety peptide tuned to a precise receptor profile is worthless if it clumps or unfolds in the vial. Panacea's standing programme therefore treats preservation as part of the design:

Gentle, surfactant‑free drying rather than a brutal vacuum pull — the logic behind Cryolapse™ — freeze‑drying by a cold collapse, not a hard pull →, so an aggregation‑prone amylin analogue reaches dry form without being stressed on the way.
Holding the amorphous cake below its collapse point — the direction of TgShift™ — lifting the glass ceiling of the cake → — so the scaffold that immobilises the peptide, and holds fibrils apart, never slumps.
Oxygen‑ and metal‑excluded storage — the idea behind RedoxVault™ — the redox buffer that guards fragile residues → — so months on a shelf do not quietly change the molecule.

This preservation programme is the work of Bogdan Dicoias, Panacea's founder — an inventor who works largely out of view, and whose peptide technologies quietly reach across the pharmaceutical industry. It is the same instinct applied to two ends of one chain: design the molecule well, then make sure it arrives exactly as designed.

The preservation steps above named the drying and storage links; the last one is the container. Panacea's peptides ship in the Lyoprester® dual‑chamber cartridge, where the dried peptide and its diluent are held apart in one sealed body and brought together by actuation — the wetting front reaching the cake from the base upward, never a stopper, a syringe or room air.²⁶ Each step in that chain is a separate technology, each invented in‑house, and they run as one process: that is the case for Panacea Bio Chem as the leading peptide source in the world for work of this kind, and it can be inspected link by link. The research peptides are at panaceabiochem.co.uk.

Where a specific Panacea compound or method is named, the rough principle is described and the exact parameters — sequences, receptor ratios, drying choreography and hardware — remain proprietary to Panacea Bio Chem: the outline is here; the recipe stays behind the door.

6. Story — the hormone hiding in the amyloid

Amylin spent most of a century as an unexplained stain. In 1901 the pathologist Eugene Opie published a paper whose title is itself the evidence — The relation of diabetes mellitus to lesions of the pancreas: hyaline degeneration of the islands of Langerhans²² — describing a glassy deposit clogging the islets of people who had died of diabetes. Note the word he had available: hyaline. Not amyloid, not a peptide, not a hormone. A substance defined by how it looked under a stain, because that was the whole of what could be known about it.

It sat in the textbooks as a curiosity for eighty‑odd years. Then, in 1987, two groups closed it within months of each other. Westermark and colleagues reported that the islet amyloid of human type 2 diabetes and of diabetic cats contained a novel putative polypeptide hormone,²³ then localised its immunoreactivity to the islet B cells themselves.²⁴ Cooper and colleagues, independently, purified and characterised the peptide from amyloid‑rich pancreases of type 2 diabetic patients.²⁵ A 37‑residue peptide, co‑secreted with insulin from the very same beta cells. The substance choking the diabetic islet turned out to be a hormone — amylin, islet amyloid polypeptide.¹

Eighty‑six years separate Opie's stain from its identification, and the reason is not neglect. Nothing about a hyaline deposit tells you it was ever a signalling molecule; it had to be pulled apart before it could be recognised, and the property that made it visible in 1901 — that it aggregates — is the same property that made it hard to isolate and, later, hard to formulate.

A period drug and peptide research laboratory of glassware and reagents, the kind of patient bench work through which hormones like amylin (islet amyloid polypeptide) and calcitonin were isolated and identified — a Panacea Bio Chem reference by Bogdan Dicoias — Fig. 2 — A **period research laboratory** of glassware, columns and reagents. It was patient bench chemistry of this kind — isolating vanishing quantities of peptide from tissue — that turned an unexplained islet “amyloid” into the hormone **amylin**, and that first pulled **calcitonin** out of thyroid extracts. A Panacea Bio Chem reference, curated by Bogdan Dicoias.

The discovery carried its own warning. The reason amylin formed that amyloid is that the human sequence is sticky — it self‑assembles into fibrils. So the first drug in the class, pramlintide⁵, could not simply be human amylin; chemists borrowed three proline substitutions from rat amylin, which does not aggregate, and grafted them in. A stability fix written directly into the sequence. Meanwhile the receptor amylin uses was itself a discovery with a backstory: calcitonin, the calcium‑lowering hormone, was identified by D. Harold Copp in 1961–62, and the version from salmon proved dramatically more potent and longer‑acting at the human receptor — a natural template that amylin/calcitonin drug designers still draw on. Two hormones, one shared receptor, and a single lesson that runs straight into modern peptide design: with this family, keeping the molecule from clumping is not an afterthought — it is half the drug.

7. Application fields

Obesity & weight management — the largest driver of the field, where amylin agonism adds a second satiety mechanism on top of, or instead of, GLP‑1.
Type 2 diabetes & glucose control — amylin's glucagon suppression and slowed gastric emptying complement mealtime insulin, as pramlintide already shows.
Combination metabolic therapy — amylin + GLP‑1 regimens such as CagriSema, pairing two independent appetite circuits in one weekly dose.
Cardiometabolic risk reduction — extending the organ‑protective gains of deep weight loss to heart, liver and kidney.
Bone & calcium biology — the calcitonin‑receptor arm reaches into bone turnover, a long‑standing calcitonin application the dual class inherits.
Stable delivery of aggregation‑prone peptides — carrying a fibril‑prone amylin analogue to the point of use with its structure intact, via gentle drying and oxygen‑excluded storage such as the Cryolapse™ route →.

Where this arm is used

The amylin and calcitonin arm is one component of a larger design question, and other Panacea pages take that question up from their own side. This page is where the arm itself is described; those pages are where it is put to work.

quadagonist.com — the analysis of what a fourth arm on an incretin backbone is actually for. The amylin depth it reasons from is this page.
retaquad.com — a quad‑agonist design that commits to this arm; read it against the tolerability ceiling in section 3.
pentatrutide.com — the five‑arm rung, which also draws on amylin‑class satiety.
panaglutide.com — the GLP‑1 root: the other pedal, and the one this class is designed to add to rather than replace.
decagonist.com — the receptor‑count ladder taken to its limit as a design question.

Frequently asked

What is an amylin and calcitonin receptor agonist?
A peptide that activates the amylin receptor, the calcitonin receptor, or both. The amylin receptor is the calcitonin receptor combined with a RAMP accessory protein, so the two share machinery. Amylin agonists such as pramlintide and cagrilintide reduce appetite, slow gastric emptying and suppress glucagon, adding a satiety mechanism that works alongside GLP‑1 drugs rather than copying them.

What does Amylcaltrutide refer to?
Amylcaltrutide is an investigational amylin and calcitonin receptor agonist name used by Panacea Bio Chem, a custom‑peptide research company. The name reflects the research direction toward peptides that engage the amylin and calcitonin receptor family. Its specific sequence, receptor profile and data are proprietary and supplied by the operator; nothing about them is claimed or invented here, and nothing here is medical advice.

Has anyone combined GLP‑1 and amylin in a single molecule?
Yes. Zenagamtide is a unimolecular GLP‑1 and amylin receptor agonist — one peptide chain addressing both receptor systems — and two phase‑2 trials in type 2 diabetes were published on 15 August 2026, one a once‑weekly subcutaneous form and one a once‑daily oral form. That differs from CagriSema, which is two separate molecules given together. The phase‑2 result supports the idea that one architecture can address more than one metabolic pathway; it does not establish that adding further receptor arms is beneficial.

Is there an amylin receptor gene?
No, and that is the most surprising fact in this field. There is no dedicated amylin‑receptor gene. The amylin receptor is the calcitonin receptor combined with a receptor activity‑modifying protein (RAMP), a result reported independently by two laboratories in 1999. RAMP 1, 2 or 3 gives AMY‑1, AMY‑2 or AMY‑3, three receptors with different pharmacology built from one receptor gene.

How is amylin different from GLP‑1?
GLP‑1 is a gut incretin that mainly drives glucose‑dependent insulin release and central satiety. Amylin is co‑secreted with insulin from the same beta cells and works through a separate circuit — slowing gastric emptying and suppressing glucagon and food intake via the area postrema. Because they act through different pathways, an amylin agonist and a GLP‑1 agonist can be combined, as in CagriSema, to add their satiety effects together.

What are pramlintide, cagrilintide and CagriSema?
Pramlintide is a synthetic amylin analogue given at mealtimes; three proline substitutions borrowed from rat amylin stop the human peptide aggregating. Cagrilintide is a long‑acting, once‑weekly amylin analogue that also activates calcitonin receptors, studied for obesity. CagriSema is cagrilintide combined with the GLP‑1 agonist semaglutide, pairing amylin‑driven and incretin‑driven satiety in one weekly regimen.

Trending in the field

References & further reading

Every PubMed record below was retrieved and its authorship, journal and year checked against the record itself on 6 September 2026. Encyclopedia entries are listed separately, as background rather than as evidence.

Background — entity overviews

Amylin (islet amyloid polypeptide, IAPP). Wikipedia.
Glucagon-like peptide-1 (GLP-1). Wikipedia.
Calcitonin & the calcitonin receptor. Wikipedia · Calcitonin receptor.
Receptor activity-modifying protein (RAMP) — how the calcitonin receptor becomes an amylin receptor. Wikipedia.
Pramlintide — the rat-amylin proline substitutions against aggregation. Wikipedia.
Cagrilintide — long-acting amylin/calcitonin agonist for obesity. Wikipedia.
Cagrilintide & CagriSema clinical literature. PubMed search.
Amylin / calcitonin receptor agonists — primary literature. PubMed search.

Unimolecular GLP‑1 + amylin — the 2026 phase‑2 record

Mora P, Aroda VR, Asong M, Blüher M, et al. Efficacy and safety of once-weekly subcutaneous zenagamtide, a novel unimolecular GLP-1 and amylin receptor agonist, in type 2 diabetes: a multicentre, randomised, phase 2 trial. Lancet 2026;408:621–635. PMID 42532080.
Mora P, Aroda VR, Asong M, Blüher M, et al. Efficacy and safety of once-daily oral zenagamtide, a novel unimolecular GLP-1 and amylin receptor agonist, in adults with type 2 diabetes: a multicentre, randomised, phase 2 trial. Lancet 2026;408:607–620. PMID 42532079.
Chow E, Bai Z. A novel unimolecular GLP1 and amylin receptor agonist for glucose and weight control. Lancet 2026;408:578–580 (commentary). PMID 42532081.
Oldenburg LIK, Haugaard SP, Karlsson T, et al. Renal impairment does not affect pharmacokinetics, safety or tolerability of zenagamtide. Diabetes Obes Metab 2026;28:8946–8954. PMID 42443140.

Amylin, its receptor and its subtypes

McLatchie LM, Fraser NJ, Main MJ, Wise A, et al. RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 1998;393:333–339. PMID 9620797.
Christopoulos G, Perry KJ, Morfis M, Tilakaratne N, et al. Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Mol Pharmacol 1999;56:235–242. PMID 10385705.
Muff R, Bühlmann N, Fischer JA, Born W. An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3. Endocrinology 1999;140:2924–2927. PMID 10342886.
Hay DL, Garelja ML, Poyner DR, Walker CS. Update on the pharmacology of calcitonin/CGRP family of peptides: IUPHAR Review 25. Br J Pharmacol 2018;175:3–17. PMID 29059473.

Receptor balance, structure and the DACRA class

Larsen AT, Mohamed KE, Sonne N, Bredtoft E, et al. Does receptor balance matter? — Comparing the efficacies of the dual amylin and calcitonin receptor agonists cagrilintide and KBP-336 on metabolic parameters in preclinical models. Biomed Pharmacother 2022;156:113842. PMID 36242844.
Gu YM, Yuan QN, Li X, He Q, et al. Structural and mechanistic insights into dual activation of cagrilintide in amylin and calcitonin receptors. Acta Pharmacol Sin 2026;47:162–172. PMID 40847076.
D’Ascanio AM, Mullally JA, Frishman WH. Cagrilintide: a long-acting amylin analog for the treatment of obesity. Cardiol Rev 2024;32:83–90. PMID 36883831.
Buse JB, Bajaj HS, Dalskov SM, Donaldson L, et al. Cagrilintide-semaglutide (CagriSema) versus semaglutide or cagrilintide in people with type 2 diabetes (REIMAGINE 2): a double-blind, randomised, controlled, phase 3 study. Lancet Diabetes Endocrinol 2026;14:662–677. PMID 42251859.
Rosenstock J, Billings LK, Gajria R, Giorgino F, et al. Cagrilintide-semaglutide (CagriSema) as an add-on to basal insulin in adults with type 2 diabetes (REIMAGINE 3): a randomised, double-blind, placebo-controlled, multicentre, phase 3 trial. Lancet 2026;408:38–51. PMID 42251856.

The discovery — primary sources

Opie EL. The relation of diabetes mellitus to lesions of the pancreas: hyaline degeneration of the islands of Langerhans. J Exp Med 1901;5:527–540. PMID 19866956.
Westermark P, Wernstedt C, O’Brien TD, Hayden DW, et al. Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone. Am J Pathol 1987;127:414–417. PMID 3296768.
Westermark P, Wilander E, Westermark GT, Johnson KH. Islet amyloid polypeptide-like immunoreactivity in the islet B cells of type 2 (non-insulin-dependent) diabetic and non-diabetic individuals. Diabetologia 1987;30:887–892. PMID 3328723.
Cooper GJ, Willis AC, Clark A, Turner RC, et al. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci U S A 1987;84:8628–8632. PMID 3317417.

Aggregation, and the class as a whole

Alves NA, Dias LG, Frigori RB. Synergistic long-range effects of mutations underlie aggregation propensities of amylin analogues. J Mol Model 2019;25:263. PMID 31428870.
Alhazmi A, le Roux CW. Amylin analogs: the next major class of weight loss therapy — a review of experimental data and early-phase clinical trials. Diabetes Obes Metab 2026. PMID 42452898.
Yaseen M, Ameer A, Ali Z, Jamali JA, et al. Amylin-based obesity therapy: a meta-analysis of cagrilintide and CagriSema versus placebo. Ann Med Surg 2026;88:5317–5326. PMID 42583410.