Also known as IAPP · Islet amyloid polypeptide · Pramlintide (analog) · Symlin
The pancreas’s second satiety hormone — co-secreted with insulin from the beta cell; its stabilized analog pramlintide treats diabetes, and the class now drives a new wave of obesity drugs.
Research refreshed
Amylin is a 37-amino-acid hormone released alongside insulin from the pancreatic beta cells, where it slows gastric emptying, suppresses glucagon, and promotes satiety — complementing insulin’s glucose-lowering action. Native human amylin is sticky and aggregation-prone (it forms the islet amyloid seen in type 2 diabetes), so the therapeutic is the soluble analog pramlintide (Symlin); the longer-acting analog cagrilintide, profiled separately in this catalog, has pushed the class to the front of obesity drug development.
Insulin is famous; the hormone the beta cell co-secretes with it is not. Amylin (islet amyloid polypeptide) is released in the same secretory granules and handles the parts of glucose control insulin does not: it puts a brake on gastric emptying so nutrients arrive more slowly, it suppresses the inappropriate glucagon that drives post-meal sugar spikes, and it signals fullness to the brain. In effect amylin and insulin are a co-secreted pair, much as glucagon is insulin’s counter-hormone.
The molecule has a notorious second identity. Human amylin is amyloidogenic — it misfolds and aggregates into the islet amyloid deposits found in type 2 diabetes, which is both a manufacturing headache and a disease-relevant feature. That stickiness is why the native hormone cannot simply be bottled: pramlintide swaps three residues (prolines that block aggregation) to create a stable, soluble analog usable as an injectable adjunct to insulin in type 1 and type 2 diabetes.
The forward-looking story is obesity. Because amylin signaling curbs appetite through a pathway distinct from the incretins, long-acting amylin analogs — led by cagrilintide — are being combined with GLP-1 drugs (e.g. cagrilintide plus semaglutide) and are posting some of the largest weight-loss figures in current trials. Amylin is a hormone that spent decades as insulin’s overlooked partner and is now a primary target in its own right.
Agonist at the amylin receptor (a calcitonin-receptor core complexed with receptor-activity-modifying proteins, RAMPs). It slows gastric emptying, suppresses postprandial glucagon, and acts centrally to reduce food intake.
Behind every vial of Amylin is the same exacting pipeline every research peptide runs — but the chemistry plays out differently for this molecule. Here is how Amylin, specifically, is brought into being.
On paper, Amylin weighs in at roughly 3,903.3 daltons. Before a single bond is made, the target sequence, salt form, and purity threshold are written down as the contract the finished material must meet.
Amylin's chain is short but unusual — it carries non-natural residues that help it resist enzymatic breakdown, but demand specialized, costlier building blocks and careful coupling on the synthesizer. It also carries a disulfide bridge, an extra step beyond a plain chain that adds both capability and cost.
The crude mixture — Amylin plus its deletions and side products — is then separated on preparative HPLC, and where the cut is taken decides the difference between a genuinely pure peptide and a barely-passable one.
A real batch of Amylin proves itself: identity confirmed by mass spectrometry against its ~3,903.3 Da, purity read directly off an analytical HPLC trace, water and counterion content measured. That batch-specific certificate of analysis is the only honest way to know what is actually in a vial of Amylin — and a short, cold, accountable chain of custody is how that purity survives the trip to your bench.
A 37-residue, 2–7-disulfide, C-terminal-amide peptide and one of the hardest sequences in this class to make: native human amylin is intrinsically amyloidogenic, so it aggregates on the resin and in solution. The therapeutic pramlintide is the design answer — three proline substitutions (Ala25, Ser28, Ser29 → Pro) that break the β-sheet stacking, simultaneously making the peptide synthesizable, soluble, and shelf-stable. It is the catalog’s clearest example of engineering *against* aggregation to obtain a manufacturable peptide; the longer-acting analog cagrilintide (profiled separately) extends the same logic.
Don't judge a vial by its cake. A fluffy, good-looking lyophilized powder reflects bulking agents and freeze-drying parameters — not purity. Insist on a batch-specific certificate of analysis.
Recent clinical trials and publications mentioning Amylin, pulled automatically from ClinicalTrials.gov and PubMed and refreshed daily. Listings are unfiltered search results, not curated endorsements.
A hormone co-secreted with insulin from the pancreatic beta cells that slows gastric emptying, suppresses glucagon, and promotes satiety — handling parts of glucose control that insulin does not.
Pramlintide (Symlin) is a synthetic amylin analog with three amino-acid substitutions that prevent the aggregation seen with native human amylin, making it stable enough to use as an injectable add-on to insulin.
Amylin curbs appetite through a pathway separate from the GLP-1 incretins, so long-acting amylin analogs such as cagrilintide — especially combined with GLP-1 drugs — produce large weight-loss effects in trials.
No — this is a research and educational reference, not dosing guidance.
Dosing protocols, mechanism, comparisons, and the latest trials — citation-backed answers grounded in PubMed, PubChem, and ClinicalTrials.gov.