
A short chain of amino acids linked by peptide bonds, often functioning as a signaling molecule or hormone.Peptides are short chains of amino acids linked by peptide bonds, typically ranging from two to about fifty amino acids in length. They occupy a middle ground between individual amino acids and full proteins, yet they are not merely smaller versions of proteins — they have their own distinct biological roles. Many hormones, such as insulin and oxytocin, are peptides, as are numerous signaling molecules that coordinate cellular activity, immune responses, and even appetite regulation. Because they are small and often highly specific, peptides can act quickly and be broken down easily, making them ideal for transient regulatory tasks in the body.
The term 'peptide' was coined in the early 20th century, and the first peptide hormone, insulin, was sequenced by Frederick Sanger in the 1950s, which earned him the Nobel Prize in Chemistry.
A peptide forms when the carboxyl group of one amino acid reacts with the amino group of another, releasing a water molecule and creating a peptide bond. The sequence of amino acids determines the peptide's shape and function; even a small change in sequence can drastically alter its activity. Once synthesized, a peptide can bind to specific receptors on cell surfaces, triggering a cascade of intracellular events that change cell behavior. Their short length means they often adopt simple structures, such as loops or helices, which are well-suited for binding to receptor pockets.
Peptides are used in medicine as hormones, antibiotics, and vaccines, and in research as tools to study protein interactions and cell signaling.
Some peptides, like the antimicrobial peptides found in frog skin, can kill bacteria by poking holes in their membranes, and they are being studied as alternatives to conventional antibiotics.






