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Chemical structure of thiostrepton, a thiopeptide

Thiopeptides (thiazolyl peptides) are a class of peptide antibiotics produced by bacteria. They have antibiotic activity against Gram-positive bacteria, but little or no activity against Gram-negative bacteria.[1] Many of the members of this class show activity against methicillin-resistant Staphylococcus aureus (MRSA) and are therefore subjects of research interest.[citation needed]

There are over 100 members of this class known.[2]

Chemical structure[edit]

Thiopeptides are sulfur-rich macrocyclic peptides containing highly-modified amino acids. They are characterized by a nitrogen-containing six-membered ring (such as piperidine, dehydropiperidine, or pyridine) substituted with multiple thiazole rings and dehydroamino acids.[3] A macrocylic ring serves as a scaffold for a tail that also incorporates modified amino acids often with azole rings, such as thiazoles, oxazoles, and thiazolines which are derived from serine, threonine, and cysteine residues.[3]


Examples of thiopeptides include thiostrepton, cyclothiazomycin, nosiheptide, and lactocillin.[citation needed]


  1. ^ Bagley, Mark C.; Dale, James W.; Merritt, Eleanor A.; Xiong, Xin (2005). "Thiopeptide Antibiotics". Chemical Reviews. 105 (2): 685–714. doi:10.1021/cr0300441. PMID 15700961.
  2. ^ "THIOBASE: a Database of Thiopeptides Featured in Genetics and Chemistry".
  3. ^ a b Just-Baringo, X; Albericio, F; Álvarez, M (2014). "Thiopeptide Antibiotics: Retrospective and Recent Advances". Marine Drugs. 12 (1): 317–351. doi:10.3390/md12010317. PMC 3917276. PMID 24445304.