General Information
-
DRAMP ID
- DRAMP02275
-
Peptide Name
- Ranacyclin-T (Frogs, amphibians, animals)
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Source
- Rana temporaria (European common frog)
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Family
- Belongs to the frog skin active peptide family (Brevinin subfamily)
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Gene
- RNCT
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Sequence
- GALRGCWTKSYPPKPCK
-
Sequence Length
- 17
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UniProt Entry
- P83719
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
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Target Organism
-
- [Ref.14636071]Gram-positive bacteria: Bacillus megaterium Bm11 (MIC=3 µM), Staphylococcus lentus (MIC=10 µM), Micrococcus luteus (MIC=8 µM);
- Gram-negative bacteria: Escherichia coli D21 (MIC=30 µM), Yersinia pseudotuberculosis YP III (MIC=5 µM), Pseudomonas syringae pv tabaci (MIC=16 µM);
- Fungi: Candida albicans ATCC 10231 (MIC=22 µM), Candida tropicalis (MIC=14 µM), C. guillermondii (MIC=1 µM), Phytophthora nicotianae spores (MIC=16 µM).
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Hemolytic Activity
-
- [Ref.14636071] It has 20% hemolytic activity at 100 μM against human erythrocytes
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Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
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Binding Target
- Cell membrane
Structure Information
-
Linear/Cyclic
- Cyclic
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N-terminal Modification
- Free
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C-terminal Modification
- Amidation
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Nonterminal Modifications and Unusual Amino Acids
- Disulfide bond between Cys6 and Cys16.
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Stereochemistry
- L
-
Structure
- Not found
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- Please click DRAMP02275_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C85H134N24O21S2
Absent Amino Acids
- DEFHIMNQV
Common Amino Acids
- KP
Mass
- 1892.27
PI
- 9.7
Basic Residues
- 4
Acidic Residues
- 0
Hydrophobic Residues
- 3
Net Charge
- +4
-
Boman Index
- -24.18
Hydrophobicity
- -0.877
Aliphatic Index
- 28.82
Half Life
-
- Mammalian:30 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 7115
Absorbance 280nm
- 444.69
Polar Residues
- 7
DRAMP02275
Comments Information
MOA
- The mature peptide inserts into the hydrophobic core of the bacterial cell membrane and increases permeability without disrupting membrane integrity. Probably binds to the outer membrane surface before aggregating to form transmembrane pores. Has hemolytic activity.
Literature Information
- ·Literature 1
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Title
- Ranacyclins, a new family of short cyclic antimicrobial peptides: biological function, mode of action, and parameters involved in target specificity.
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Pubmed ID
- 14636071
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Reference
- Biochemistry. 2003 Dec 2;42(47):14023-14035.
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Author
- Mangoni ML, Papo N, Mignogna G, Andreu D, Shai Y, Barra D, Simmaco M.