Making peptides one bond at a time in solution was slow. Each step needed careful purification, so long chains took months or years.
In 1963 Bruce Merrifield published a new approach. He anchored the first amino acid to a tiny solid bead of resin. Further amino acids were added one at a time, and excess reagents were simply washed away after each step. This solid-phase method made peptide synthesis faster and easier to automate. Merrifield received the 1984 Nobel Prize in Chemistry for it.
Later prizes show how far the tools have come. In 2012 Robert Lefkowitz and Brian Kobilka shared the Nobel Prize in Chemistry for studies of G-protein-coupled receptors. These receptors sit in cell membranes, and many of them respond to peptide messengers. In 2017 Jacques Dubochet, Joachim Frank and Richard Henderson shared the prize for developing cryo-electron microscopy, which images frozen biomolecules in near-atomic detail.
In 2024 the prize went half to David Baker for computational protein design, and half to Demis Hassabis and John Jumper for protein structure prediction. Their AlphaFold models can predict a chain's three-dimensional shape from its sequence alone.
Today, a researcher can write a sequence, build the chain on a machine, predict its shape with software and check it with a microscope. That would have seemed impossible to Fischer in 1901.
References
- NobelPrize.org, Bruce Merrifield: Facts, Nobel Prize in Chemistry (1984)
- NobelPrize.org, The Nobel Prize in Chemistry 2017 (2017)
- NobelPrize.org, The Nobel Prize in Chemistry 2024 (2024)
Educational content about laboratory research. Not medical advice. All Orion compounds are for laboratory research use only.
