Peptides are biologically active molecules, consisted of short chains of amino acid monomers linked together via amide bonds (–CONH–). These molecules are attractive building blocks in bioorganic and supramolecular chemistry due to available diversity of amino acid sequences and their predictable conformational properties.
Emil Fischer, along with Ernest Fourneau, synthesized the first synthetic peptide[1], ‘dipeptide’—glycylglycine, in 1901. This is considered as beginning of peptide chemistry. Progress however was slow for the next 50 years. Therefore medicinal use of synthetic peptides started after the Second World War. In 1953, the chemical synthesis of the first polypeptide—‘oxytocin’ by du Vigneaud was a milestone in peptide [2] history.
However, amount of time and effort that peptide synthesis took was enormous by conventional methods. In 1963, Bruce Merrifield accelerated and automated this long process using the method he named Solid Phase Peptide Synthesis (SPPS). SPPS method paved the way for simple, rapid and effective preparation of peptides and small proteins. This technological leap has remarkably sparked progress in biochemistry, molecular biology, pharmacology and medicine. With their excellent specificity which is transferred into remarkable safety, tolerability and efficacy, peptides became an excellent starting point for the design of novel therapeutics.
[1] Fischer E, Fourneau E (1901) Ubereinige derivate des glykocolls. Ber Dtsch Chem Ges 34:2868–2877.
[2] Suresh Babu VV (2001) One hundred years of peptide chemistry. Resonance 6(10):68.