General Information
-
DRAMP ID
- DRAMP01646
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Peptide Name
- Adenoregulin (Dermaseptin BII; Dermaseptin B2; Frogs, amphibians, animals)
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Source
- Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor)
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Family
- Belongs to the frog skin active peptide family (Dermaseptin subfamily)
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Gene
- ADR
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Sequence
- GLWSKIKEVGKEAAKAAAKAAGKAALGAVSEAV
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Sequence Length
- 33
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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.8306981]Fungi: Microsporum canis (IP 1194) (MIC=10 µg/ml), Tricophyton rubrum (IP 1400-82) (MIC=15 µg/ml), Arthroderma simii (IP 1063-74) (MIC=30 µg/ml), Aspergillus fumigatus IP (1025-70) (MIC=125 µg/ml), Aerornonas caviae (IP 67-16 T) (MIC=60 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=15 µg/ml);
- Gram-negative bacterium: Escherichia coli (IP 76-24) (MIC=15 µg/ml);
- Gram-positive bacterium: Nocardia brasiliensis (IP 16-80) (MIC=30 µg/ml).
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Hemolytic Activity
-
- [Ref:8306981]Lack hemolytic activity against rabbit red blood cells
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Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Linear
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N-terminal Modification
- Free
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C-terminal Modification
- Free
-
Nonterminal Modifications and Unusual Amino Acids
- Free
-
Stereochemistry
- L
-
Structure
- Alpha helix
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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 DRAMP01646_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C142H242N40O42
Absent Amino Acids
- CDFHMNPQRTY
Common Amino Acids
- A
Mass
- 3181.73
PI
- 9.7
Basic Residues
- 6
Acidic Residues
- 3
Hydrophobic Residues
- 18
Net Charge
- +3
-
Boman Index
- -7.65
Hydrophobicity
- 0.197
Aliphatic Index
- 95.15
Half Life
-
- Mammalian:30 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 5500
Absorbance 280nm
- 171.88
Polar Residues
- 6
DRAMP01646
Comments Information
Fountion
- Enhances binding of agonists to adenosine A1 receptors, adenosine A2a receptors, alpha-2 adrenergic receptors and 5-hydroxytryptamine 1A receptors. Enhances guanyl nucleotide exchange which may result in the conversion of receptors to a high affinity state complexed with guanyl nucleotide free G-protein. Affects human behavior eliciting profound malaise, followed by listlessness and then euphoria. Possesses a potent antimicrobial activity against bacteria, fungi and protozoa. Lack hemolytic activity. Probably acts by disturbing membrane functions with its amphipathic structure.
Tissue specificity
- Expressed by the skin glands.
PTM
- C-terminal amidation at V33 (Amidation in vitro increases antimicrobial activity against some microorganisms such as T. album and S. cerevisia).
Literature Information
- ·Literature 1
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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, 219 (1-2):145-154.
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Author
- Mor, A, Nicolas, P.
- ·Literature 2
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Title
- Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor.
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Pubmed ID
- 1438301
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Reference
- Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10960-10963.
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Author
- Daly JW, Caceres J, Moni RW, Gusovsky F, Moos M Jr, Seamon KB, Milton K, Myers CW.
- ·Literature 3
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Title
- Effects of the amphiphilic peptides mastoparan and adenoregulin on receptor binding, G proteins, phosphoinositide breakdown, cyclic AMP generation, and calcium influx.
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Pubmed ID
- 7842473
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Reference
- Cell Mol Neurobiol. 1994 Apr;14(2):133-157.
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Author
- Shin Y, Moni RW, Lueders JE, Daly JW.
- ·Literature 4
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Title
- The amphiphilic peptide adenoregulin enhances agonist binding to A1-adenosine receptors and [35S]GTP gamma S to brain membranes.
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Pubmed ID
- 8565049
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Reference
- Cell Mol Neurobiol. 1995 Aug;15(4):465-493.
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Author
- Moni RW, Romero FS, Daly JW.