General Information
-
DRAMP ID
- DRAMP01668
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Peptide Name
- Dermaseptin-1 (DS I; Dermaseptin-S1, DS1; Frogs, amphibians, animals)
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Source
- Phyllomedusa sauvagei (Sauvage's leaf frog)
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Family
- Belongs to the frog skin active peptide family (Dermaseptin subfamily)
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Gene
- Not found
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Sequence
- ALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ
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Sequence Length
- 34
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiprotozoal
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Target Organism
-
- Fungi: Microsporum canis (IP 1194) (MIC=50 µg/ml), Tricophyton rubrum (IP 1400-82) (MIC=100 µg/ml), Arthroderma simii (IP 1063-74) (MIC=100 µg/ml), Aspergillus fumigatus (IP 1025-70) (MIC=100 µg/ml), Aerornonas caviae IP (67-16) T (MIC=50 µg/ml), Cryptococcus neoformans (IP 960-67) (MIC=15 µg/ml), Cryptococcus neoformans (IP 962-67) (MIC=15 µg/ml), Candida albicans (IP 884-65) (MIC=60 µg/ml);
- Gram-negative bacterium: Escherichia coli (IP 76-24) (MIC=5 µg/ml);
- Gram-positive bacterium: Nocardia brasiliensis (IP 16-80) (MIC=200 µg/ml).
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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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
- Linear
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N-terminal Modification
- Free
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C-terminal Modification
- Free
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Nonterminal Modifications and Unusual Amino Acids
- Free
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Stereochemistry
- L
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Structure
- Alpha helix (CD)
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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 DRAMP01668_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C152H257N43O44S2
Absent Amino Acids
- CEFNPRVY
Common Amino Acids
- A
Mass
- 3455.09
PI
- 10
Basic Residues
- 5
Acidic Residues
- 1
Hydrophobic Residues
- 15
Net Charge
- +4
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Boman Index
- -5.55
Hydrophobicity
- 0.185
Aliphatic Index
- 92.35
Half Life
-
- Mammalian:4.4 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 5500
Absorbance 280nm
- 166.67
Polar Residues
- 9
DRAMP01668
Comments Information
Function
- Possesses a potent antimicrobial activity against bacteria, fungi and protozoa. Probably acts by disturbing membrane functions with its amphipathic structure. This peptide could also inhibit HIV infection at a concentration that is also toxic to T cells (J Virol 2005; 79
Tissue specificity
- Expressed by the skin glands.
Literature Information
- ·Literature 1
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Title
- Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin.
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Pubmed ID
- 1909573
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Reference
- Biochemistry. 1991 Sep 10;30(36):8824-8830.
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Author
- Mor A, Nguyen VH, Delfour A, Migliore-Samour D, Nicolas P.
- ·Literature 2
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Title
- Isolation and structure of novel defensive peptides from frog skin.
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Pubmed ID
- 8306981
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Reference
- Eur J Biochem. 1994 Jan 15;219(1-2):145-154.
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Author
- Mor A, Nicolas P.