Temporin A
Shortest known natural antimicrobial peptide from frog skin with potent activity against gram-positive bacteria.
Chemical Identity
| Property | Value |
|---|---|
| Chemical Formula | C64H118N16O13 |
| Molecular Weight | 1319 Da |
| Peptide Class | Amphibian Antimicrobial Peptide |
| Sequence | FLPLIGRVLSGIL-NH2 |
| Origin | Rana temporaria (European frog) |
Structure
Temporin A is a 13-amino acid amphipathic alpha-helical peptide, one of the shortest natural antimicrobial peptides known. It is amidated at the C-terminus and has a net positive charge of +2. The short length makes it an attractive template for synthetic optimization.
Mechanism of Action
Temporin A disrupts bacterial membranes through its amphipathic alpha-helical structure. It preferentially targets gram-positive bacteria by interacting with anionic phospholipids (phosphatidylglycerol, cardiolipin) abundant in gram-positive membranes. The peptide forms pores causing membrane depolarization and lysis.
Clinical Applications
- Lead compound: Template for short AMP design
- Topical formulations: Potential for skin infections
- Anti-MRSA: Active against methicillin-resistant staphylococci
- Synergy studies: Enhanced activity with other AMPs
Pharmacology
- Spectrum: Primarily gram-positive bacteria
- Hemolysis: Low at antimicrobial concentrations
- Length: Minimal effective length for AMP activity
- Salt sensitivity: Partially affected by divalent cations
References
- Simmaco, M., et al. (1996). Temporins: antimicrobial peptides from Rana temporaria skin. Biochemical and Biophysical Research Communications, 229, 697-702.
- Wade, D., et al. (2000). Structure-activity analysis of temporin A. European Journal of Biochemistry, 267, 3624-3630.
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