Blog
A Short History of Peptide Drugs: From Insulin to GLP-1
Peptides feel like a new topic, but the first peptide medicine is more than a century old. Following the history shows why the field looks the way it does: first extracting, then synthesizing, then engineering.
Key takeaways
- Insulin in the 1920s was the first peptide hormone used as a medicine.
- Chemical synthesis became practical after oxytocin in 1953 and solid-phase methods in 1963.
- Recombinant DNA replaced animal-extracted insulin in the 1980s.
- Engineering for long half-life produced today’s GLP-1 class.
1921 to 1923: insulin
In 1921, Frederick Banting and Charles Best, working in John Macleod’s laboratory in Toronto, showed that a pancreatic extract lowered blood sugar in diabetic dogs. James Collip helped purify the extract for human use, and the first patient was treated in 1922. The 1923 Nobel Prize in Physiology or Medicine went to Banting and Macleod. Insulin was then made by extraction from animal pancreas, in limited and variable quantities.
1950s: structure and the first synthesis
Frederick Sanger worked out the complete amino acid sequence of insulin by 1955, earning the 1958 Nobel Prize in Chemistry. Vincent du Vigneaud isolated and synthesized oxytocin in 1953, the first synthetic polypeptide hormone, and won the 1955 Nobel Prize in Chemistry. Together, these showed that peptides had defined sequences that chemistry could reproduce.
1963: solid-phase synthesis
Bruce Merrifield’s resin-based method made it practical to assemble peptides step by step without purifying after every reaction. He received the Nobel Prize in Chemistry in 1984. Our post on how peptides are made walks through the process.
1980s: recombinant insulin
In 1982, recombinant human insulin made in bacteria became the first biotechnology medicine approved, ending reliance on animal extracts and proving that cells could be programmed to make peptides.
1990s to 2000s: analogs and incretins
- GnRH analogs such as leuprolide showed that small sequence edits could turn a short-lived hormone into a long-acting therapy.
- Teriparatide, a fragment of parathyroid hormone, was approved in 2002.
- Exenatide, based on a peptide from the saliva of the Gila monster, was approved in 2005 and opened the GLP-1 era.
2010s to today: engineered half-life
Natural GLP-1 lasts only minutes because the enzyme DPP-4 destroys it. Liraglutide, approved in 2010, attached a fatty acid to bind albumin. Semaglutide, approved in 2017, added further protection against DPP-4 and a longer fatty chain. Tirzepatide, approved in 2022, is a dual-receptor design acting on GIP and GLP-1 receptors. The tricks behind these steps are explained in how researchers make peptides last longer, and the research context is in our semaglutide research summary.
What the history teaches
- Almost every step involved fixing a weakness: supply, purity, stability or half-life.
- Peptide medicines succeeded when manufacturing and analytics caught up with biology.
- Quality control, the topic of much of our Research Library, is not an add-on. It is why the field works.
The bottom line
The modern research peptide catalog sits at the end of a long chain of innovations in extraction, synthesis and design. Products sold by Lucid Aminos are for laboratory research use only and are not approved medicines.
Related reading
- How Peptides Are Made: Solid-Phase Synthesis from Resin to Vial
- How Researchers Make Peptides Last Longer: D-Amino Acids, Acylation and More
- Semaglutide Research: What the Current Data Shows
- Browse the full Research Library
For laboratory research use only. Not for human or veterinary use, and not intended to diagnose, treat, cure or prevent any condition. This article is educational and is not medical advice.