PR-39
Porcine proline-rich antimicrobial peptide that inhibits bacterial protein synthesis and promotes wound healing through non-lytic mechanisms.
Chemical Identity
| Property | Value |
|---|---|
| Chemical Formula | C155H260N56O34 |
| Molecular Weight | 3720 Da |
| Peptide Class | Proline-rich Antimicrobial Peptide |
| Sequence | RRRPRPPYLPRPRPPPFFPPRLPPRIPPGFPPRFPPRFP-NH2 |
| Origin | Porcine neutrophils |
Structure
PR-39 is a 39-amino acid proline-rich peptide isolated from porcine neutrophils. It contains 49% proline and 15% arginine residues, giving it an unusual extended polyproline helix conformation. This structure enables non-membranolytic mechanisms of action and cellular uptake.
Mechanism of Action
Unlike membrane-disrupting AMPs, PR-39 enters bacterial cells and inhibits protein synthesis by binding to ribosomal proteins and blocking translation. It also has important non-antimicrobial functions: promoting wound healing, angiogenesis, and inhibiting NADPH oxidase assembly in inflammatory cells.
Clinical Applications
- Wound healing: Promotes fibroblast migration and angiogenesis
- Anti-inflammatory: Inhibits NADPH oxidase and superoxide production
- Cardiovascular protection: Reduces ischemia-reperfusion injury
- Lead compound: Bacitracin analogs inspired by proline-rich AMPs
Pharmacology
- Spectrum: Primarily gram-negative bacteria
- Mechanism: Non-lytic (intracellular targets)
- Uptake: Enters mammalian and bacterial cells
- Half-life: Short in plasma (protease sensitive)
References
- Agerberth, B., et al. (1991). PR-39: a proline-rich antibacterial peptide from pig intestine. European Journal of Biochemistry, 202, 849-854.
- Gallo, R.L., et al. (1994). PR-39: wound healing and angiogenesis. Proceedings of the National Academy of Sciences, 91, 11035-11039.
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