Thiopeptides are a growing class of sulfur-rich, highly modified heterocyclic peptide antibiotics. According to our survey, the thiopeptide family now contains near 100 entities, all of which possess a characteristic macrocyclic core that consists of a monoaza six-membered ring central to multiple thiazoles and dehydroamino acids but vary in side chains (and/or rings) that append additional functionalities. The clinical interest in this family was recently renewed, since many members show potent activity against various drug-resistant pathogens, including methicillin-resistant Staphylococcus aureus, penicillin-resistant Streptococcus pneumoniae and vancomycin-resistant Enterococcus. Interestingly, specific activity has been newly reported against certain cancer cells, like targeting the transcription factor FOXM1. This motivates extensive investigations by chemical modification into new analogue development; however, their complex architecture poses a tremendous challenge to synthetic ways.

To date there are ten biosynthetic gene clusters of thiopeptides published. These studies substantiate a unifying rationale: The structural complexity of all thiopeptides probably arises from unforeseen posttranslational modifications of genetically encoded and ribosomally translated peptides.

Herein, we carry out a comprehensive survey and therefore constitute a web-based database THIOBASE, relevant to "Chemical & Genetic Characterization of Thiopeptide Antibiotic" to document the information regarding thiopeptides in structure, producing system and featured biosynthetic gene, aiming at expediting of new thiopeptide discovery and accumulating of specific building elements for applying combinatorial biosynthesis methods to meet the requirement of diversity for drug discovery and development.