• • DRAMP ID

  • DRAMP01646

• • Peptide Name

  • Adenoregulin (Dermaseptin BII; Dermaseptin B2; Frogs, amphibians, animals)

• • Source

  • Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor)

• • Family

  • Belongs to the frog skin active peptide family (Dermaseptin subfamily)

• • Gene

  • ADR

• • Sequence

  • GLWSKIKEVGKEAAKAAAKAAGKAALGAVSEAV

• • Sequence Length

  • 33

• • UniProt Entry

  • P31107,P80283

• • Protein Existence

  • Protein level

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal

• • 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).

• • Hemolytic Activity

  • • [Ref:8306981]Lack hemolytic activity against rabbit red blood cells

• • Cytotoxicity

  • No cytotoxicity information found in the reference(s) presented

• • Binding Target

  • Not found

• • Linear/Cyclic

  • Linear

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Free

• • Nonterminal Modifications and Unusual Amino Acids

  • Free

• • Stereochemistry

  • L

• • Structure

  • Alpha helix

• • Structure Description

  • Not found

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP01646.

DRAMP01646

• • 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 1

• • Title

  • Isolation and structure of novel defensive peptides from frog skin.

• • Pubmed ID

  • 8306981

• • Reference

  • Eur J Biochem 1994, 219 (1-2):145-154.

• • Author

  • Mor, A, Nicolas, P.

• ·Literature 2

• • Title

  • Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor.

• • Pubmed ID

  • 1438301

• • Reference

  • Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10960-10963.

• • Author

  • Daly JW, Caceres J, Moni RW, Gusovsky F, Moos M Jr, Seamon KB, Milton K, Myers CW.

• ·Literature 3

• • Title

  • Effects of the amphiphilic peptides mastoparan and adenoregulin on receptor binding, G proteins, phosphoinositide breakdown, cyclic AMP generation, and calcium influx.

• • Pubmed ID

  • 7842473

• • Reference

  • Cell Mol Neurobiol. 1994 Apr;14(2):133-157.

• • Author

  • Shin Y, Moni RW, Lueders JE, Daly JW.

• ·Literature 4

• • Title

  • The amphiphilic peptide adenoregulin enhances agonist binding to A1-adenosine receptors and [35S]GTP gamma S to brain membranes.

• • Pubmed ID

  • 8565049

• • Reference

  • Cell Mol Neurobiol. 1995 Aug;15(4):465-493.

• • Author

  • Moni RW, Romero FS, Daly JW.