What type of reaction leads to the formation of peptide bonds?

The formation of peptide bonds occurs through a process known as a condensation reaction. In this type of reaction, two amino acids come together, and a molecule of water is released as a byproduct. This occurs when the amino group of one amino acid reacts with the carboxyl group of another, forming the peptide bond and linking the two amino acids together into a dipeptide.

While condensation and dehydration reactions are closely related (both involve the loss of water), the term "condensation reaction" is more generally used to describe the process of joining smaller molecules to form larger ones while eliminating water. Therefore, recognizing the primary characteristic of linking amino acids via peptide bond formation fits best under the definition of a condensation reaction, which underscores the main chemical change involved.

Hydrolysis reactions, on the other hand, involve the addition of water to break down larger molecules into smaller ones, so they are not relevant to bond formation. Oxidation reactions focus on the transfer of electrons and changing the oxidation states of molecules, which is not applicable to the peptide bond formation context.