Peptide Schedule
Amylin (IAPP)37 residuesKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYEach bubble = one amino acid. Size = residue mass. Color = chemical class.Amylin (IAPP) Dosage Calculator
Amylin, also known as islet amyloid polypeptide (IAPP), is a 37-amino-acid peptide hormone produced by pancreatic beta cells and co-secreted with insulin in response to nutrient stimuli.
10mcg · 3x Daily
Summary: Add 2mL BAC water to your 1mg vial. Draw to 2.0 units on a U-100 syringe for a 10mcg dose. This vial will last 100 doses.
Cycle Planner
Amylin (IAPP) Pharmacokinetics
Pharmacokinetics — Active Dose Over Time
t½ = ~13-22 minutesDisclaimer: This curve is a simplified first-order exponential decay model. Actual pharmacokinetics vary based on injection site, individual metabolism, body composition, and other factors. Half-life values are approximate and based on available preclinical and clinical literature. Many research peptides lack formal human pharmacokinetic studies. This is for educational purposes only — not medical advice.
Amylin (IAPP) Dosing Protocol
| Level | Dose / Injection | Frequency |
|---|---|---|
| Beginner | 10mcg | 3x Daily |
| Moderate | 25mcg | 3x Daily |
| Aggressive | 50mcg | 3x Daily |
Note: Research-only peptide. Native human amylin (islet amyloid polypeptide, IAPP) is a 37-amino-acid peptide hormone co-secreted with insulin from pancreatic beta cells. It plays a key physiological role in glucose homeostasis, but its tendency to aggregate into amyloid fibrils limits clinical use. The FDA-approved analog pramlintide (Symlin) has three proline substitutions that prevent aggregation. Cagrilintide is a next-generation long-acting amylin analog in late-stage development. Native amylin is used in research settings to study amyloid formation, beta-cell toxicity, and metabolic signaling.
About Amylin (IAPP)
Amylin, also known as islet amyloid polypeptide (IAPP), is a 37-amino-acid peptide hormone produced by pancreatic beta cells and co-secreted with insulin in response to nutrient stimuli. Discovered in 1987 by Garth Cooper and colleagues from amyloid deposits in the pancreas of type 2 diabetics, amylin was quickly recognized as a physiologically important hormone with multiple roles in glucose homeostasis. In healthy individuals, amylin complements insulin through three distinct mechanisms: it slows gastric emptying via vagal signaling, suppresses postprandial glucagon secretion from pancreatic alpha cells, and promotes satiety through receptors in the area postrema and hypothalamus. These actions collectively flatten the postprandial glucose curve, reducing the demand on insulin. In type 1 diabetes, amylin production is lost entirely along with beta cells. In type 2 diabetes, amylin secretion is initially elevated but becomes progressively impaired as beta cells fail. The clinical challenge with native amylin is its strong propensity to misfold and aggregate into toxic amyloid fibrils. This amyloidogenesis is central to the pathology of type 2 diabetes — IAPP-derived amyloid deposits are found in the islets of over 90% of type 2 diabetes patients at autopsy and contribute to beta-cell death. The key amyloidogenic region spans residues 20-29, with residues S20-S29 forming a beta-sheet structure that nucleates fibril formation. Because native amylin cannot be used therapeutically due to aggregation, pramlintide was developed with three proline substitutions (A25P, S28P, S29P) that disrupt beta-sheet formation while preserving receptor activity. Pramlintide was FDA-approved in 2005 as adjunctive therapy for insulin-treated diabetes. The next-generation analog cagrilintide (developed by Novo Nordisk) uses acylation technology to extend the half-life to approximately one week, enabling weekly dosing and improved adherence. Native amylin remains an extensively studied research tool for understanding amyloid biology, neurodegenerative diseases (IAPP amyloid shares structural similarities with amyloid-beta in Alzheimer's), and metabolic signaling pathways. It is not used therapeutically.