Peptide bond

A **peptide bond** is a covalent amide linkage that joins the carboxyl group of one amino acid with the amino group of another, releasing a molecule of water in a condensation (dehydration synthesis) reaction[1][3][7]. It is the fundamental chemical linkage forming polypeptides and proteins, connecting amino acids into their linear sequence, also known as the primary structure of proteins[1][3][7]. The peptide bond is strong, rigid, and planar due to partial double-bond character, which restricts rotation and contributes to the stability and folding of proteins[1][3][4]. Peptide bonds are not receptors, enzymes, transporters, or typical therapeutic targets but are instead structural chemical bonds vital for the formation of all peptides and proteins[1][2][3][7]. The term “peptide bond” does not denote a discrete biological molecule, receptor, or drug target; its role is chemical, not pharmacological, and so it is not targeted directly by drugs but may be cleaved by proteolytic enzymes such as proteases. **Key clarification:** "Peptide bond" is not a therapeutic target (such as a receptor, enzyme, channel, or transporter); it is a type of chemical bond found universally in all proteins and peptides. It does not have a canonical abbreviation, is not associated with aliases beyond chemical nomenclature (e.g., "amide bond"), has no direct disease roles, drug interactions, or mechanisms of action, and is not used as a biomarker or associated with safety concerns. Therefore, most fields are not applicable or return null for structured target data, and the entry is **incorrect as a therapeutic/pharmacological target**[1][2][3][7].

Other names

Eupeptide bondAmide bond (context-dependent, see description)

Not applicable