📚 Wiki Antimicrobial & Immune Temporin

Temporin

● Preclinical
Rana Temporaria Skin Antimicrobial Peptide
Also known as: temporin-A, temporin-B, temporin-L, frog skin AMP
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Quick Summary

Temporins are a family of short (10-14 amino acid) cationic antimicrobial peptides isolated from the skin secretions of the European common frog (Rana temporaria). First described by Simmaco et al.

Antimicrobial Peptide Preclinical
Temporins are a family of short (10-14 amino acid) cationic antimicrobial peptides isolated from the skin secretions of the European common frog (Rana temporaria). First described by Simmaco et al. in 1996, they are among the smallest naturally occurring antimicrobial peptides, yet show broad-spectrum activity against Gram-positive bacteria, fungi, and protozoa. Temporins adopt amphipathic alpha-helical conformations in membrane-mimetic environments and disrupt microbial membranes with selectivity over mammalian cells.
Storage Stability
Lyophilized
1–2 years (-20°C)
Reconstituted
~30 days (2–8°C)
Room temp
Avoid

Mechanism of Action

Membrane Disruption at Low Charge

Unlike magainins (+4 charge), most temporins have low positive charge (+1 to +3) yet are antimicrobial. They compensate with high hydrophobicity and a compact helix that inserts efficiently into bacterial membranes. The mechanism is primarily carpet-like membrane disruption rather than discrete pore formation. Temporin-L (the most active family member) has +3 charge and strong hydrophobicity, giving activity against Gram-negative bacteria as well.

Synergistic Combinations

Individual temporins often show narrow-spectrum activity (primarily Gram-positive). However, combinations of temporin-A and temporin-B show synergistic activity against Gram-negative bacteria. This synergy arises from sequential membrane destabilization: temporin-B disrupts the outer membrane, allowing temporin-A access to the inner membrane. Temporin combinations thus broaden the spectrum beyond individual members.


Research Summary

Activity Against Biofilms

Preclinical

Temporin-A is notable for activity against Staphylococcus epidermidis biofilms at concentrations similar to its planktonic MIC, unlike many antibiotics with poor biofilm penetration. In mouse catheter-associated biofilm models, temporin-A coating reduces biofilm colonization. These properties are relevant for medical device coatings and wound dressings.

Antifungal and Antiparasitic Activity

Preclinical

Several temporin variants show activity against Candida spp. and Leishmania parasites. Temporin-A and temporin-B disrupt Candida albicans biofilms and planktonic cells. Anti-Leishmania activity involves disruption of the parasite plasma membrane and mitochondrial membrane potential, with selectivity over mammalian cells.

Structural Optimization

Preclinical

Due to their short length, temporins are attractive scaffolds for medicinal chemistry optimization. D-amino acid substitutions, C-terminal amidation (already present in natural forms), and hybrid peptides with other AMP sequences have been explored to improve spectrum, stability, and selectivity. Several temporin analogs show enhanced Gram-negative activity while maintaining low hemolytic toxicity.


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Research Protocols

GoalDoseFrequencyRoute
Antibacterial MIC determination1-128 ug/mLSingle plate readIn vitro (broth microdilution)
Biofilm prevention (catheter coating)10-100 ug/mL coating concentrationSingle applicationSurface coating
Anti-Leishmania activity1-50 uMSingle time-pointIn vitro (parasite suspension)

All protocols are research context only. No clinical development for temporins as standalone antibiotics. Used primarily as AMP scaffold and mechanistic tool.


Interactions

synergistic
Temporin-A + Temporin-B combination
Sequential membrane disruption extends spectrum to Gram-negative bacteria; well characterized synergy
complementary
Both are frog skin AMPs; different charge/hydrophobicity profiles; comparative tool for AMP mechanism studies
additive/synergistic
Conventional antibiotics (gentamicin, ampicillin)
Membrane permeabilization by temporin enhances conventional antibiotic uptake into bacteria

Safety Profile

Temporins are hemolytic at concentrations above their antimicrobial range, particularly temporin-L which has high hemolytic activity. Temporin-A shows better selectivity with a therapeutic index (HC50/MIC) of ~10-50 for Staphylococcus. No human clinical data exists. Use is restricted to research and potential topical/local applications where systemic absorption is minimal. Not available as a human therapeutic.


References

  • [1]Simmaco M, et al. Temporins, antimicrobial peptides from the European red frog Rana temporaria. Eur J Biochem. 1996;242(3):788-792.
  • [2]Mangoni ML, et al. Temporins and their synergism against Gram-negative bacteria and in lipopolysaccharide detoxification. Biochim Biophys Acta. 2008;1778(12):2620-2627.
  • [3]Di Grazia A, et al. D-amino acid analogues of temporin-L are highly efficient antimicrobial agents. Sci Rep. 2015;5:12518.
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Data Sources & External References
Source: peer-reviewed literature  ·  Domain: ascendpeptide.org

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