Cinnamycin

Cinnamycin

Cinnamycin (also known as Ro 09-0198) is a peptide antibiotic that is produced by the bacterium Streptomyces cinnamoneus. It is a member of the duramycin family of antibiotics and is known for its ability to bind to phosphatidylethanolamine (PE), a phospholipid found in the membranes of cells.

Structure

Cinnamycin is a 19-amino acid peptide with a unique lasso structure. This structure is characterized by a macrolactam ring that is threaded by the C-terminal tail of the peptide. The lasso structure is stabilized by a network of hydrogen bonds and van der Waals forces, which contribute to the peptide's stability and resistance to protease degradation.

Mechanism of Action

Cinnamycin's mechanism of action is unique among peptide antibiotics. It binds specifically to PE, a phospholipid that is normally located on the inner leaflet of the cell membrane. When cells undergo apoptosis or are damaged, PE is exposed on the cell surface. Cinnamycin binds to this exposed PE, disrupting the cell membrane and leading to cell death.

Clinical Use

While cinnamycin is not currently used in clinical practice, it has potential therapeutic applications. Its ability to bind to exposed PE could be used to target cancer cells, which often have PE on their surface. Additionally, cinnamycin could be used to target bacteria that have PE in their membranes.

Research

Research into cinnamycin and related peptides is ongoing. Studies have focused on understanding the structure and function of these peptides, as well as exploring their potential therapeutic uses.

See Also

• Duramycin
• Phosphatidylethanolamine
• Peptide antibiotics
• Streptomyces cinnamoneus

References

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