• • DRAMP ID

  • DRAMP03002

• • Peptide Name

  • Melittin (Allergen Api m 3; Allergen Api m III; Insects, animals)

• • Source

  • Apis mellifera (Honeybee)

• • Family

  • Belongs to the melittin family

• • Gene

  • MELT

• • Sequence

  • GIGAVLKVLTTGLPALISWIKRKRQQ

• • Sequence Length

  • 26

• • UniProt Entry

  • P01501,P01503

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • [Ref.29783753] Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=2 μM), Listeria monocytogenes CMCC 54004 (MIC=1 μM);
    • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1 μM), Escherichia coli UB 1005 (MIC=2 μM), Salmonella pullorum C7913 (MIC=8 μM), Salmonella enterica subsp enterica CMCC 50071 (MIC=2 μM)

• • Hemolytic Activity

  • • [Ref.29859288] MHC=1 μM against human red blood cell.
    • [Ref.2978375] 46.80% hemolysis at 2μM against human red blood cell
    • [Ref.20472009] Wild-type melittin:AVG ± S.D.(%)=0.077±0.002 (35) against human red blood cell.

• • Cytotoxicity

  • • Not included yet

• • Binding Target

  • Cell membrane (forms a transmembrane alpha-helix in the cell membrane.)

• • Linear/Cyclic

  • Not included yet

• • N-terminal Modification

  • Not included yet

• • C-terminal Modification

  • Not included yet

• • Nonterminal Modifications and Unusual Amino Acids

  • Not included yet

• • Stereochemistry

  • Not included yet

• • Structure

  • Alpha helix

• • Structure Description

  • Not found

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 2MLT,3QRX,1BH1

• Predicted Structure

• There is no predicted structure for DRAMP03002.

DRAMP03002

• • Function

  • Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na+-K+-ATPase and the H+-K+-ATPase. It increases the permeability of cell membranes to ions, particularly Na+ and indirectly Ca2+, because of the Na+-Ca2+-exchange. It acts synergistically with phospholipase A2.

• ·Literature 1

• • Title

  • Expression in Escherichia coli of novel recombinant hybrid antimicrobial peptide AL32-P113 with enhanced antimicrobial activity in vitro.

• • Pubmed ID

  • 29859288

• • Reference

  • Gene. 2018 May 30. pii: S0378-1119(18)30617-6.

• • Author

  • Wanmakok M, Orrapin S, Intorasoot A, Intorasoot S.

• ·Literature 2

• • Title

  • Broad-Spectrum Antimicrobial Activity and Low Cytotoxicity against Human Cells of a Peptide Derived from Bovine AlphaS1-Casein.

• • Pubmed ID

  • 29783753

• • Reference

  • Molecules. 2018 May 19;23(5). pii: E1220.

• • Author

  • Hou J, Liu Z, Cao S, Wang H, Jiang C, Hussain MA, Pang S.

• ·Literature 3

• • Title

  • Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin.

• • Pubmed ID

  • 6309516

• • Reference

  • Eur J Biochem. 1983 Sep 1;135(1):123-126.

• • Author

  • Vlasak R, Unger-Ullmann C, Kreil G, Frischauf AM.

• ·Literature 4

• • Title

  • Identification of a novel melittin isoform from Africanized Apis mellifera venom.

• • Pubmed ID

  • 20472009

• • Reference

  • Peptides. 2010 Aug;31(8):1473-1479.

• • Author

  • Sciani JM, Marques-Porto R, Louren?o Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC.

• ·Literature 5

• • Title

  • Africanized honey bee (Apis mellifera) venom profiling: Seasonal variation of

• • Pubmed ID

  • 20403370

• • Reference

  • Toxicon. 2010 Sep 1;56(3):355-362.

• • Author

  • Ferreira Junior RS, Sciani JM, Marques-Porto R, Junior AL, Orsi Rde O, Barraviera B, Pimenta DC.

• ·Literature 6

• • Title

• • Pubmed ID

  • 5300771

• • Reference

  • Res Dev Tech Rep. 1967 Dec 5:1-13.

• • Author

  • Fennell JF, Shipman WH, Cole LJ.