How does a peptide bond form between two amino acids?

A peptide bond forms through a condensation reaction between two amino acids. During this process, an –OH group is removed from the carboxyl group of one amino acid, while a hydrogen atom is removed from the amino group of a second amino acid.1

This reaction results in the release of a molecule of water and creates a covalent bond between the carbon atom of the first amino acid's carboxyl group and the nitrogen atom of the second amino acid's amino group. This linkage is known as an amide or peptide bond.12

In living cells, this process is catalyzed by ribosomal RNA within the ribosome, which facilitates the peptidyl transferase reaction to link amino acids into chains. Once joined, the individual amino acids are referred to as amino acid residues.31