Details

Autor(en) / Beteiligte

• Tran, Thao Thi Phuong
• Huynh, Ni Ngoc Thi
• Pham, Ninh Thi
• Nguyen, Dung Thi
• Tran, Chien Van
• Nguyen, Uyen Quynh
• Ho, Anh Ngoc
• Suh, Joo-Won
• Cheng, Jinhua
• Nguyen, Thao Kim Nu
• Tran, Sung Van
• Nguyen, Duc Minh

Titel

Metabolites from Streptomyces aureus (VTCC43181) and Their Inhibition of Mycobacterium tuberculosis ClpC1 Protein

Ist Teil von

• Molecules (Basel, Switzerland), 2024-02, Vol.29 (3), p.720

Ort / Verlag

Switzerland: MDPI AG

Erscheinungsjahr

2024

Quelle

MEDLINE

Beschreibungen/Notizen

• Tuberculosis is one of the most common infectious diseases in the world, caused by . The outbreak of multiple drug-resistant tuberculosis has become a major challenge to prevent this disease worldwide. ClpC1 is a Clp ATPase protein of , functioning as a chaperon when combined with the Clp complex. ClpC1 has emerged as a new target to discover anti-tuberculosis drugs. This study aimed to explore the ClpC1 inhibitors from actinomycetes, which have been known to provide abundant sources of antibiotics. Two cyclic peptides, including nocardamin ( ), halolitoralin A ( ), and a lactone pleurone ( ), were isolated from the culture of (VTCC43181). The structures of these compounds were determined based on the detailed analysis of their spectral data and comparison with references. This is the first time these compounds have been isolated from Compounds - were evaluated for their affection of ATPase activity of the recombinant ClpC1 protein. Of these compounds, halolitoralin A ( ), a macrocyclic peptide, was effective for the ATPase hydrolysis of the ClpC1 protein.