When Were Peptides Discovered and By Who? The History of Peptide Science from 1901 to Modern Research
Peptides are now central to modern biochemistry, molecular biology, endocrinology, neuroscience, metabolic research, and biotechnology. They are studied as cell-signaling molecules, hormone fragments, mitochondrial messengers, structural research tools, receptor ligands, and biochemical standards. But peptide science did not begin with modern synthetic laboratories or today's GLP-1 research boom. It began more than 120 years ago with one of the most important chemists of the early twentieth century: Emil Fischer.
The first laboratory-made peptide was synthesized in 1901 by Emil Fischer and Ernest Fourneau, who created glycylglycine, a dipeptide made from two glycine amino acids. In 1902, Fischer introduced the term "peptide", using language derived from Greek words associated with digestion and protein breakdown products. This work established the foundation of peptide chemistry and helped scientists understand that amino acids could be linked together through what became known as the peptide bond.
Source note: Fischer and Fourneau synthesized glycylglycine in 1901; Fischer introduced the term peptide in 1902. Sources: IAS Resonance article on one hundred years of peptide chemistry; EL3VATE history of peptide science.
Today, more than a century later, peptide research includes everything from classic molecules such as insulin, oxytocin, and glutathione, to newer research peptides such as MOTS-c, BPC-157, TB-500, GHK-Cu, CJC-1295, Ipamorelin, AOD-9604, KPV, LL-37, Semax, Selank, and GLP-1-related research compounds. For research-use-only products and educational resources, visit the BlueNexLabs product collection and Research Hub.
What Are Peptides?
Peptides are short chains of amino acids joined by peptide bonds. In general, peptides are smaller than proteins, although the boundary between a large peptide and a small protein can vary depending on scientific context. Peptides may contain only two amino acids, as in the first synthesized peptide glycylglycine, or dozens of amino acids, as seen in many naturally occurring signaling peptides.
In biological research, peptides are studied because they can act as:
· Cell-signaling molecules
· Hormones or hormone fragments
· Enzyme substrates
· Receptor-binding ligands
· Antioxidant-related molecules
· Immune and inflammatory pathway research tools
· Mitochondrial-derived signaling molecules
· Structural models for protein chemistry
This is why peptides are so important in modern molecular research. They are small enough to synthesize, modify, and study, but biologically specific enough to interact with receptors, enzymes, and signaling pathways.
The Early Discovery of Peptides: Emil Fischer and the Birth of Peptide Chemistry
1901: Emil Fischer and Ernest Fourneau synthesize the first peptide
The modern history of peptides begins in 1901, when German chemist Emil Fischer and French chemist Ernest Fourneau synthesized glycylglycine. Glycylglycine is a simple dipeptide composed of two glycine amino acids. While simple by today's standards, this discovery was revolutionary because it showed that amino acids could be linked together chemically in a laboratory. At the time, proteins were still poorly understood. Scientists knew that proteins were essential to living systems, but they did not yet have a clear chemical explanation for how amino acids were arranged or connected. Fischer's peptide work helped establish that proteins and peptides were not random substances but structured molecules built through specific chemical bonds.
1902: The word “peptide” is introduced
In 1902, Fischer introduced the term peptide during a scientific meeting in Karlsbad. The term referred to smaller protein-like fragments produced during digestion or chemical breakdown of proteins. Fischer's terminology became the standard language of peptide chemistry and remains in use today. Fischer later synthesized longer peptide chains, including an 18-amino-acid peptide, which was an extraordinary achievement for early twentieth-century chemistry. His work earned him recognition as one of the founders of modern peptide and protein chemistry.
Early Peptide Hormone Discoveries
1902: Secretin and the birth of hormone science
In the same period that Fischer was defining peptide chemistry, physiologists were discovering that the body uses chemical messengers to communicate between organs. In 1902, British physiologists William Bayliss and Ernest Starling discovered secretin, a substance released by the small intestine that stimulates pancreatic secretion. Secretin is historically important because it became recognized as the first hormone ever identified. This discovery changed biology. Before secretin, many scientists believed that organ-to-organ communication was controlled almost entirely by nerves. Secretin showed that chemical messengers in the bloodstream could also coordinate biological activity. This opened the door to peptide hormone research.
1905: Gastrin is proposed
In 1905, John Sydney Edkins proposed the existence of gastrin, a digestive hormone involved in gastric acid regulation. Gastrin became another early example of how peptide-like signaling molecules helped explain communication within the gastrointestinal system. These discoveries helped establish the gut as one of the most important endocrine systems in the body -- a concept that later became essential to GLP-1 research.
Insulin: The Peptide That Changed Medicine and Research
1921-1922: Insulin is isolated in Toronto
One of the most famous peptide discoveries occurred at the University of Toronto in 1921, when Frederick Banting, Charles Best, John Macleod, and James Collip isolated insulin from pancreatic tissue. In January 1922, insulin was administered to Leonard Thompson, a 14-year-old patient with Type 1 diabetes, marking one of the most important milestones in medical history. Insulin became the first peptide-based substance to demonstrate life-saving therapeutic potential in humans. Its discovery proved that peptides were not just chemical curiosities; they could be powerful biological regulators. For peptide researchers, insulin also became a model molecule. It helped scientists understand structure-function relationships, peptide sequencing, hormone signaling, purification methods, and later recombinant biotechnology.
Frederick Sanger and the First Complete Protein Sequence
1951-1955: Insulin is sequenced
British biochemist Frederick Sanger determined the complete amino acid sequence of insulin, making insulin the first protein ever fully sequenced. This work showed that proteins and peptides have exact amino acid sequences rather than random arrangements. Sanger's insulin sequencing work was so important that he received the 1958 Nobel Prize in Chemistry. This discovery helped launch modern molecular biology because it proved that biological function could be linked to a precise amino acid sequence.
Oxytocin and the First Synthetic Peptide Hormone
1953: Vincent du Vigneaud synthesizes oxytocin
In 1953, American biochemist Vincent du Vigneaud synthesized oxytocin, a nine-amino-acid peptide hormone. This was the first time a peptide hormone had been fully synthesized in a laboratory while retaining the activity of the natural molecule. Du Vigneaud's work demonstrated that peptide hormones could be chemically manufactured and that a synthetic peptide could match its naturally occurring counterpart. He received the 1955 Nobel Prize in Chemistry for this landmark achievement. This breakthrough paved the way for modern peptide synthesis, research peptides, peptide analogues, and peptide-based biotechnology.
1963: Solid-Phase Peptide Synthesis Changes Everything
Before the 1960s, peptide synthesis was slow and difficult. Each amino acid had to be added, purified, and verified through labor-intensive solution chemistry. In 1963, Robert Bruce Merrifield introduced Solid-Phase Peptide Synthesis, often abbreviated as SPPS. SPPS involved anchoring the growing peptide chain to an insoluble resin support so amino acids could be added step by step without isolating every intermediate. This dramatically improved speed, efficiency, reproducibility, and automation potential. Merrifield later received the 1984 Nobel Prize in Chemistry for this achievement. Most modern synthetic peptide manufacturing still relies on principles derived from Merrifield's SPPS method.
Source note: Insulin, Sanger sequencing, du Vigneaud oxytocin synthesis, and Merrifield SPPS are widely documented milestones in peptide science. Sources include Pepperpedia summaries, EBSCO Research Starters, and historical peptide chemistry references.
GLP-1 Peptides: Discovery, Location, and Why They Became So Important
Early 1980s: GLP-1 is discovered through proglucagon gene research
One of the most important peptide discoveries of the late twentieth century was Glucagon-Like Peptide-1, commonly known as GLP-1. GLP-1 was identified in the early 1980s during research on the proglucagon gene. Scientists found that the gene encoding glucagon also contained sequences for other related peptides, including GLP-1 and GLP-2. Early work included studies on anglerfish, hamster, human, and rat proglucagon genes by researchers including Joel Habener, Graeme Bell, and their colleagues.
The GLP-1 story is geographically important because it involved multiple research centres. Work connected to GLP-1 discovery and characterization included laboratories at Massachusetts General Hospital/Harvard, the University of Toronto, and the University of Copenhagen, among others.
1986-1987: The biologically active GLP-1 fragment is characterized
After GLP-1 sequences were identified in proglucagon genes, researchers needed to determine which GLP-1 forms existed in tissues and which forms were biologically active. Svetlana Mojsov, working in peptide chemistry and radioimmunoassay development, contributed to identifying and detecting GLP-1 peptides, including active truncated GLP-1 forms.
By the mid-to-late 1980s, GLP-1 had been characterized as an incretin hormone involved in glucose-regulated insulin secretion. The discovery and characterization of GLP-1 later became the foundation for one of the most important areas of metabolic peptide research.
Why GLP-1 matters in peptide history
GLP-1 is important because it represents a bridge between classic peptide hormone discovery and modern engineered peptide analogues. Natural GLP-1 is rapidly broken down in the body, which led researchers to develop modified GLP-1 receptor agonists with longer activity. The modern GLP-1 research era has helped bring peptide science into mainstream public awareness.
Source note: GLP-1 discovery and characterization involved proglucagon gene cloning, peptide chemistry, tissue detection, and incretin biology; key people include Joel Habener, Svetlana Mojsov, Daniel Drucker, Jens Juul Holst, and Graeme Bell. Sources: Glucagon.com GLP-1 overview; Journal of Clinical Investigation review by Drucker, Habener, and Holst; Diabetes Care historical editorial.
Russian Peptide Research: A Separate and Important Chapter
Peptide research in Russia and the former Soviet Union developed along a somewhat different path than peptide research in North America and Western Europe. While Western programs often focused on hormones, endocrine peptides, and drug development, Soviet and Russian researchers placed strong emphasis on short regulatory peptides, neuropeptides, tissue-derived peptide fractions, and peptide bioregulators.
Beginning in the 1970s and 1980s, Russian researchers studied peptide compounds related to immune regulation, stress biology, cognition, neuroprotection, tissue signaling, and aging-related biological processes. A major figure in Russian peptide bioregulator research was Vladimir Khavinson, associated with peptide research at institutes in St. Petersburg.
Russian peptide research is often associated with compounds such as Epitalon, Thymalin, Thymogen, Cortexin, Vesugen, Visoluten, Semax, and Selank. Some of these became widely known in Russia and surrounding countries, while remaining relatively unfamiliar in Western medicine and regulatory systems.
Semax: A Russian ACTH-derived research peptide
Semax is one of the best-known Russian peptide compounds. It was developed at the Institute of Molecular Genetics of the Russian Academy of Sciences in Moscow, beginning in the Soviet and post-Soviet research period. Semax is a synthetic heptapeptide derived from a fragment of ACTH, modified with a Pro-Gly-Pro sequence to improve stability.
Semax was reportedly approved in Russia in the 1990s and has been studied in Russian-language literature for neurological and cognitive research contexts. Some sources describe Russian approval around 1996 for nootropic and neuroprotective indications, although Western regulatory approval and large-scale Western clinical validation remain limited.
From a research perspective, Semax is frequently discussed in relation to ACTH fragment research, neurotrophic factor signaling, BDNF and NGF-related pathways, intranasal peptide delivery models, and cognitive/neuroprotection research.
Selank: A Russian tuftsin-derived research peptide
Selank is another Russian-developed peptide, also associated with the Institute of Molecular Genetics of the Russian Academy of Sciences. Selank is a synthetic analogue of tuftsin, an immunomodulatory tetrapeptide, extended with a Pro-Gly-Pro sequence for stability.
Selank has been studied in Russian research contexts related to anxiety models, stress response, immune signaling, and neurochemical pathways. Some sources describe Russian approval around 2009 as an anxiolytic agent, although Western approval and large independent clinical replication remain limited.
From a research-use-only perspective, Selank is often discussed in relation to tuftsin analogues, GABAergic pathway research, serotonin-related signaling models, enkephalin metabolism, and stress-response peptide investigation.
Epitalon, Thymalin, Thymogen, Cortexin, Vesugen, and Visoluten
Russian peptide bioregulator research also includes several tissue-specific or short regulatory peptides. Epitalon is a synthetic tetrapeptide associated with pineal peptide research and aging-related cellular signaling models. Thymalin originated from thymus-derived peptide fraction research and became one of the better-known Soviet-era peptide bioregulators. Thymogen is a short peptide related to thymic peptide research and immune-signaling studies. Cortexin is associated with brain-derived peptide fraction research and neuropeptide investigation in Russia and Eastern Europe. Vesugen and Visoluten are examples of peptide bioregulators connected with tissue-specific research models.
This Russian tradition is important historically because it shows that peptides were not only studied as hormones or metabolic agents; they were also investigated as short regulatory molecules involved in tissue communication and cellular function.
Source note: Semax and Selank are described as Russian-developed peptide compounds associated with the Institute of Molecular Genetics of the Russian Academy of Sciences; approval dates and evidence bases vary by source and remain more limited in Western literature. Sources: Peptides.fyi, Mito Labs Bali, Arctic Labs, and peptide comparison references.
Modern Peptide and Peptide-Adjacent Research Compounds
The modern peptide research field is broad. Not every molecule sold alongside peptides is technically a peptide. For example, NAD+ is not a peptide; it is a coenzyme. However, it is often studied alongside peptides in cellular energy, mitochondrial, and longevity-related research contexts. Glutathione, by contrast, is a true tripeptide composed of glutamate, cysteine, and glycine.
Glutathione: A tripeptide discovered before modern peptide chemistry
Glutathione has one of the longest histories of any small peptide-related molecule. The earliest documented observation dates to 1888, when French researcher Joseph de Rey-Pailhade described a sulfur-reactive substance in yeast and other tissues, which he called philothion. In 1921, Frederick Gowland Hopkins isolated and named glutathione, although its exact structure was debated for several years. By the late 1920s and 1930s, researchers established glutathione as a tripeptide made from glutamate, cysteine, and glycine. Glutathione is important in research because it is central to redox biology, oxidative stress models, detoxification pathways, and cellular antioxidant systems.
NAD+: Not a peptide, but important in cellular research
NAD+, or nicotinamide adenine dinucleotide, is not a peptide. It is a coenzyme involved in redox reactions, cellular metabolism, and energy biology. It is often discussed alongside peptides because of its role in mitochondrial function, metabolic signaling, and aging-related research. NAD+ was first discovered in 1906 by British biochemists Arthur Harden and William John Young, who were studying yeast fermentation. NAD+ research later expanded into vitamin B3 biology, redox chemistry, sirtuin signaling, DNA repair, and metabolic research. Because NAD+ is not a peptide, BlueNexLabs content should describe it as a peptide-adjacent cellular research molecule, not as a peptide.
MOTS-c: A mitochondrial-derived peptide discovered in 2015
MOTS-c is one of the most interesting modern peptide discoveries. It is a 16-amino-acid mitochondrial-derived peptide encoded within the mitochondrial 12S rRNA gene. MOTS-c was discovered in 2015 by researchers at the University of Southern California, including work associated with Pinchas Cohen, Changhan Lee, and colleagues. The discovery of MOTS-c challenged older assumptions that mitochondrial DNA encoded only a limited set of oxidative phosphorylation proteins, tRNAs, and rRNAs. It showed that mitochondria could also encode bioactive signaling peptides. MOTS-c is studied in relation to mitochondrial-derived peptides, AMPK signaling, metabolic stress response, exercise-mimetic research models, and cellular adaptation and aging biology.
GHK-Cu: Copper peptide research
GHK-Cu is a naturally occurring copper-binding tripeptide first identified in human plasma in the 1970s. It is widely studied in tissue remodeling, extracellular matrix research, copper transport, and cellular signaling models. GHK-Cu is one of the best-known cosmetic and cell-biology-associated peptides, although research-use-only suppliers should avoid implying treatment, healing, or cosmetic outcomes.
BPC-157: Gastric peptide fragment research
BPC-157 is a synthetic peptide fragment derived from a protective protein sequence found in gastric research models. It has been studied in preclinical models involving tissue response, inflammatory pathways, and gastrointestinal peptide signaling. Because BPC-157 is not approved as a consumer health product in Canada, it should be described strictly as a research-use-only peptide.
TB-500 and Thymosin Beta-4 research
TB-500 is commonly discussed as a synthetic peptide fragment related to Thymosin Beta-4, a naturally occurring actin-binding protein. In research contexts, thymosin-related peptides are studied for cell migration, tissue remodeling models, actin regulation, and repair-pathway signaling. Product content should avoid athletic performance, recovery, or therapeutic claims and stay within research terminology.
CJC-1295 and Ipamorelin: Growth hormone secretagogue research
CJC-1295 is a synthetic analogue related to growth hormone-releasing hormone research, while Ipamorelin is a synthetic growth hormone secretagogue peptide studied in ghrelin receptor and endocrine signaling models. These peptides are often discussed together in research contexts involving pulsatile hormone signaling, receptor selectivity, and endocrine pathway modeling.
AOD-9604: Modified growth hormone fragment research
AOD-9604 is a modified fragment based on a region of human growth hormone. It has been studied in metabolic research models, particularly relating to lipid metabolism. BlueNexLabs should describe AOD-9604 as a research compound and avoid any claim that it causes weight loss, fat loss, or body recomposition.
KPV: Short peptide research in inflammatory pathway models
KPV is a short tripeptide sequence derived from alpha-MSH-related research. It is often studied in inflammation-related signaling models, epithelial barrier research, and immune pathway systems. Because it is a small tripeptide, it provides a good example of how even very short peptide sequences can have significant biological research relevance.
LL-37: Antimicrobial peptide research
LL-37 is a human antimicrobial peptide derived from cathelicidin research. It is studied in innate immune defense, microbial interaction models, epithelial biology, and inflammatory signaling. LL-37 is scientifically important because it demonstrates how peptides can function as part of the innate immune system.
PT-141 and melanocortin pathway research
PT-141, also known as bremelanotide in pharmaceutical contexts, is related to melanocortin receptor research. For research-use-only content, BlueNexLabs should avoid sexual-function or clinical claims and describe PT-141 only in terms of melanocortin receptor pathway investigation.
DSIP: Sleep peptide research history
Delta Sleep-Inducing Peptide, or DSIP, is a neuropeptide historically studied in sleep-related research models. It remains scientifically interesting because it reflects the long-standing connection between peptide biology and nervous system signaling.
Source note: Glutathione history is linked to de Rey-Pailhade, Hopkins, and later structural work; NAD+ history begins with Harden and Young in 1906; MOTS-c was reported in 2015 by USC researchers. Sources: Codeage glutathione history; Trends in Biochemical Sciences; AboutNAD; SpartaLabs NAD+ history; Uplevel Bio and peptide wiki resources on MOTS-c.
Expanded Peptide Discovery Timeline
1888: Glutathione is first observed as “philothion”. Joseph de Rey-Pailhade described a sulfur-reactive substance in yeast and tissues, later connected to the molecule now known as glutathione.
1901: The first synthetic peptide is made. Emil Fischer and Ernest Fourneau synthesized glycylglycine, the first laboratory-made peptide.
1902: The term “peptide” is introduced. Emil Fischer introduced the term peptide, helping establish peptide chemistry as its own scientific field.
1902: Secretin is discovered. Bayliss and Starling discovered secretin, helping establish the concept of chemical hormone signaling.
1905: Gastrin is proposed. John Sydney Edkins proposed gastrin, an early peptide hormone involved in digestive signaling.
1906: NAD+ is discovered as a fermentation cofactor. Arthur Harden and William John Young identified a heat-stable factor required for yeast fermentation, later understood as NAD+.
1921-1922: Insulin is isolated and used clinically. Banting, Best, Macleod, and Collip isolated insulin at the University of Toronto, and insulin was first administered to Leonard Thompson in 1922.
1921-1935: Glutathione is named and structurally clarified. Frederick Gowland Hopkins named glutathione in 1921, and later work established it as a tripeptide composed of glutamate, cysteine, and glycine.
1953: Oxytocin becomes the first synthetic peptide hormone. Vincent du Vigneaud synthesized oxytocin, proving a peptide hormone could be built in the laboratory and retain biological activity.
1950s: Insulin sequencing transforms peptide science. Frederick Sanger determined the amino acid sequence of insulin, proving that proteins and peptides have precise sequences.
1963: Solid-phase peptide synthesis is introduced. Robert Bruce Merrifield developed SPPS, accelerating synthetic peptide production and enabling modern peptide chemistry.
1970s-1980s: Russian peptide bioregulator research expands. Soviet and Russian scientists developed extensive research programs around short regulatory peptides, tissue-specific peptide fractions, and neuropeptides.
Early 1980s: GLP-1 is identified through proglucagon gene studies. Researchers found GLP-1 sequences within the proglucagon gene, with work involving laboratories connected to Joel Habener, Graeme Bell, and others.
1986-1987: Active GLP-1 forms are characterized. Researchers including Svetlana Mojsov and colleagues helped characterize biologically active GLP-1 forms and develop assays to detect GLP-1 peptides.
1990s: Semax becomes known in Russian peptide research. Semax, an ACTH-derived heptapeptide developed in Russia, became associated with Russian nootropic and neuroprotection research. Some sources describe Russian approval in 1996.
2000s: Selank becomes known in Russian peptide research. Selank, a tuftsin-derived heptapeptide, became associated with Russian research involving stress, anxiety models, and immune-neurochemical signaling. Some sources describe Russian approval around 2009.
2015: MOTS-c is discovered. Researchers at the University of Southern California identified MOTS-c, a mitochondrial-derived peptide encoded within mitochondrial DNA.
2020s: Peptide research enters a new public-awareness era. With increasing interest in GLP-1 receptor agonists, mitochondrial peptides, copper peptides, antimicrobial peptides, and peptide bioregulators, peptide science has become one of the most visible areas of biotechnology research.
Why Peptide History Matters for Modern Research
The history of peptides shows that scientific discovery is cumulative. Fischer's 1901 glycylglycine experiment made peptide chemistry possible. Secretin and insulin showed that peptides could function as powerful biological messengers. Sanger's insulin sequencing proved that peptide and protein structure follows exact amino acid patterns. Du Vigneaud's oxytocin synthesis showed that peptide hormones could be manufactured. Merrifield's SPPS made peptide synthesis scalable. GLP-1 research showed how peptide biology could reshape modern metabolic science. MOTS-c showed that even mitochondrial DNA contains hidden peptide signals.
Related BlueNexLabs Research Resources
· Research Peptide Collection
· Peptide Storage and Handling
Conclusion: Who Discovered Peptides?
Peptides were first synthesized in 1901 by Emil Fischer and Ernest Fourneau, who created the first laboratory-made peptide, glycylglycine. Fischer introduced the term “peptide” in 1902, making him one of the most important founders of peptide chemistry.
Since then, peptide science has grown through major discoveries including secretin, insulin, oxytocin, glutathione, GLP-1, Russian regulatory peptides such as Semax and Selank, and newer mitochondrial-derived peptides such as MOTS-c. The history of peptides spans chemistry, endocrinology, neuroscience, mitochondrial biology, immune research, and cellular signaling.
More than 120 years after Fischer's first peptide synthesis, peptides remain one of the most active and important areas of modern research.
