 Cyclic peptide

A cyclic peptide contains a covalently closed ring incorporating part or all of its amino acid residue chain. A head-to-tail ring joins the usual terminal amino and carboxyl groups through a peptide bond. Other ring architectures involve side chains or different linkages, so the positions and chemical types of the closures must be specified.^[ref]

For a topology example, a linear unbranched chain of six amino acid residues has five backbone peptide bonds. Closing that chain head-to-tail adds a sixth bond and removes its free N-terminus and C-terminus. It preserves the residue order around the ring, although choosing a different residue as the written starting point does not create a new ring. This counting example does not imply that every chosen sequence readily forms such a ring.

Alpha-amanitin supplies a biological example: it combines a cyclic eight-residue framework with an additional sulfur-containing bridge. Its shape is therefore more constrained than residue count alone reveals.^[ref] Ring closure changes accessible conformations; its effects on stability, binding and biological activity depend on the particular peptide and its surroundings.