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Hormone

Insulin

Insulin is a 51-amino-acid peptide hormone that regulates blood glucose. It is the foundational peptide therapeutic and a reference point for modern peptide drug design.

By The Peptides Codex Editorial TeamIndividual review date not recorded

Page data last changed: . Chemistry registry snapshot: . Registry refreshes and identity assessments are separate from scientific content review.

Length
51 aa
Class
Hormone
Function
Glucose regulation
Context
Diabetes treatment (approved therapeutic)

First peptide therapeutic — transformed diabetes care in the 1920s.

Part of the Foundational & therapeutic peptides cluster

Overview

Insulin is a 51-amino-acid peptide hormone that regulates blood glucose. It is the foundational peptide therapeutic and a reference point for modern peptide drug design.

Source & context

Biological / chemical source: Pancreas (human/recombinant)

Primary research or clinical context: Diabetes treatment (approved therapeutic)

Structure and chains

Mature human insulin consists of an A chain (21 residues) and B chain (30 residues) linked by disulfide bonds. Recombinant production in bacteria or yeast replaced animal-sourced insulin decades ago.

Why it matters in peptide science

Insulin demonstrated that peptides can be manufactured at scale, formulated for injection, and used as lifelong therapies. Many later peptide drugs reuse lessons from insulin formulation and delivery.

Sequence

One-letter sequence commonly cited for Insulin (educational; isoforms and modifications may differ):

GIVEQCCTSICSLYQLENYCNFVNQHLCGSHLVEALYLVCGERGFFYTPKT

GIVEQCCTSICSLYQLENYCNFVNQHLCGSHLVEALYLVCGERGFFYTPKT

Insulin51 aa · C256H381N65O77S6 · ≈ 5,794 DaPEPTIDESCODEX.COMN-terminus →→ C-terminusG1I2V3E−4Q5C6C7T8S9I10C11S12L13Y14Q15L16E−17N18Y19C20N21F22V23N24Q25H26L27C28G29S30H31L32V33E−34A35L36Y37L38V39C40G41E−42R+43G44F45F46Y47T48P49K+50T51nonpolarpolaracidicbasicGly / Pronon-canonical (X)Hydropathy (Kyte–Doolittle): ▮ hydrophobic (cyan) / ▮ hydrophilic (rose) · Side-chain charge at pH 7: + / −
Insulin — Structure cardDownload SVG
G1I2V3E4Q5C6C7T8S9I10C11S12L13Y14Q15L16E17N18Y19C20N21F22V23N24Q25H26L27C28G29S30H31L32V33E34A35L36Y37L38V39C40G41E42R43G44F45F46Y47T48P49K50T51
Helical wheel projection

Residues plotted ~100° apart around an α-helix — clustering of one color reveals an amphipathic face.

Analyze sequences in the playground →

Structure & chemistry

Molecular identity & reference confidence

Source-supported reference

Reference values are taken from the cited molecular record or curated profile. A database match is not independent laboratory verification; modifications, counter-ions, and formulations can change the measured mass.

Molecular form
Insulin (source record; form not independently established)
Species
Not established by this molecular identity audit
Termini (N / C)
Not specified / Not specified

Average reference mass

Reference policy updated: 2026-10-05

Molecular formula
C256H381N65O77S6
Average reference mass
≈ 5,794
Status
Approved medicine in at least one jurisdiction (IUPHAR record)
Identifiers

Chemistry values: PubChem, IUPHAR/BPS Guide to Pharmacology · fetched 2026-10-01.

Clinical development snapshot

ClinicalTrials.gov lists 8,203 registered studies with “Insulin” as an intervention (snapshot 2026-10-01). A registry footprint is not evidence of efficacy or approval.

Registered studies
8,203
Highest phase reached
Phase 4
Active in latest 100
72
Most recent update
2026-10-01
Most recently updated studies
NCTTitlePhaseStatusUpdated
NCT07851545Early Glucose States and 72-Hour Care-Metabolic Clusters in Critically Ill Patients—completed2026-10-01
NCT06597149Effect of Transcutaneous Auricular Vagus Nerve Stimulation (taVNS) on Plasma Insulin LevelsNot applicablerecruiting2026-10-01
NCT05713799Trial of the Combination of Alpha-Lipoic Acid and Mirabegron in Women and in Men With ObesityPhase 2not yet recruiting2026-10-01
NCT06274749Effects of Urolithin A Supplementation on Glucose Metabolism in Healthy Adults 55 >= Years Old: A Randomized TNot applicablerecruiting2026-10-01
NCT06109311A Study of Orforglipron (LY3502970) in Participants With Type 2 Diabetes and Inadequate Glycemic Control With Phase 3completed2026-10-01
NCT05120544Expanding Technology-Enabled Nurse Delivered Chronic Disease CareNot applicablecompleted2026-10-01
See all on ClinicalTrials.gov →
Concentration math

Insulin — reconstitution calculator

Enter how much peptide is in the vial and how much diluent (e.g. bacteriostatic water) is added. The tool returns the resulting solution concentration — and, for any amount you type, the volume it corresponds to. This is educational arithmetic, not a dosing recommendation.

Reference form: Insulin (source record; form not independently established)Average reference mass: 5,794 Da

Syringe graduation
Solution concentration
5 mg/mL5,000 mcg/mL
mcg

Enter an amount to see the volume it corresponds to.

Educational concentration mathematics only. This tool does not recommend a dose, amount, or protocol, and nothing here is medical advice. Many peptides are not authorized by Health Canada for human use — see our reconstitution and bacteriostatic-water guides for context.

Open the Insulin calculator on its own page →

Change log

Dated observations from the data pipeline (registry flags, trial footprints, identifiers) and editorial reviews of this profile.

  1. Trials33 registered studies added on ClinicalTrials.gov (now 8203).

FAQ about Insulin

What is Insulin?+

Insulin is a 51-amino-acid peptide hormone that regulates blood glucose. It is the foundational peptide therapeutic and a reference point for modern peptide drug design.

What Canadian product status is recorded for Insulin?+

Canadian product status for Insulin has not been verified in this profile. No verified record here does not mean no authorization exists. Status depends on the product, formulation and use; consult Health Canada's product records.

What is the typical length of Insulin?+

Insulin is commonly described as approximately 51 amino acids (Hormone).

Related peptides

Bremelanotide (PT-141)
Cyclic melanocortin-receptor agonist (approved medicine)
Bremelanotide, developed as PT-141, is a cyclic seven-residue analogue of α-melanocyte-stimulating hormone that activates melanocortin receptors, with its effect on sexual desire attributed to MC3 and MC4 signalling in the brain. The FDA approved it in 2019 as Vyleesi, an on-demand subcutaneous autoinjector for premenopausal women with acquired, generalised hypoactive sexual desire disorder. Nausea occurred in 40% of phase 3 participants, and a 2024 reanalysis found effect sizes from nil to small on most trial outcomes.
GHK-Cu
Cosmetic / research peptide
GHK-Cu is the copper(II) complex of glycyl-L-histidyl-L-lysine, a tripeptide found in human plasma at about 200 ng/mL at age 20 and 80 ng/mL by 60. It has a wide cell and animal literature on collagen synthesis, wound repair and anti-inflammatory signalling, a cosmetic market built on it, and — as a 2025 review notes — a surprising absence of clinical studies. Topical use is permitted as a cosmetic; it is not an approved drug.
MOTS-c
Mitochondrial-derived peptide (research compound)
MOTS-c is a 16-amino-acid peptide (MRWQEMGYIFYPRKLR; C101H152N28O22S2, ≈2,175 Da) encoded by a short open reading frame inside the mitochondrial 12S rRNA gene. Discovered in 2015, it promoted metabolic homeostasis and reduced obesity and insulin resistance in mice, and translocates to the nucleus under metabolic stress to regulate nuclear genes. Plasma levels decline with age. It is a research compound with no approval; its first phase 2 trial, in prediabetes, was recruiting in 2026.
Vasopressin
Hormone
Vasopressin (antidiuretic hormone) is a nine-residue peptide closely related to oxytocin, central to water balance physiology.

References & further reading

  1. 1.Le et al. (2023). Insulin signaling and its application. Front Endocrinol (Lausanne)
  2. 2.Ogawa et al. (2022). New classification and diagnostic criteria for insulin resistance syndrome. Endocr J
  3. 3.Frank et al. (2014). Insulin dysregulation. Equine Vet J
  4. 4.Needham et al. (2024). Personalized phosphoproteomics of skeletal muscle insulin resistance and exercise links MINDY1 to insulin action. Cell Metab
  5. 5.Lechleitner et al. (2011). Insulin therapy. Wien Med Wochenschr
  6. 6.Simpson et al. (1999). Insulin aspart. Drugs
  7. 7.Rhea et al. (2024). Insulin and the blood-brain barrier. Vitam Horm
  8. 8.Waldhäusl (1992). [Insulin resistance]. Acta Med Austriaca
  9. 9.PubChem — compound summary for Insulin Human (CID 118984375)
  10. 10.Wikipedia — Insulin
Disclaimer: Educational content only. Not medical advice. Not instructions for human use. Research peptides and unapproved products may be restricted or illegal to market for human consumption in your jurisdiction. Consult qualified professionals and applicable law.
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