• • DRAMP ID

  • DRAMP03748

• • Peptide Name

  • Bradykinin-potentiating peptide BmK3 (Bpp BmK3; NDBP-3.3; Arthropods, animals)

• • Source

  • Mesobuthus martensii (Manchurian scorpion) (Buthus martensii)

• • Family

  • Belongs to the scorpion BPP family

• • Gene

  • Not found

• • Sequence

  • FRFGSFLKKVWKSKLAKKLRSKGKQLLKDYANKVLNGPEEEAAAPAE

• • Sequence Length

  • 47

• • UniProt Entry

  • Q9Y0X4

• • Protein Existence

  • Transcript level

• • Biological Activity

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

• • Target Organism

  • • [Ref.22115565]Gram-negative bacteria: Escherichia coli DH 5-α (MIC=2.3 µM), Haemophilus influenzae ATCC 31517 (MIC=3.2 µM), Klebsiella pneumoniae ATCC 13882 (MIC=2.8 µM), Salmonella enterica ATCC 8090 (MIC=2.3 µM), Pseudomonas aeruginosa ATCC 9229 (MIC=4.7 µM), Serratia marcescens ATCC 13880 (MIC=68.2 µM);
    • Gram-positive bacteria: Bacillus subtilis ATCC 6051 (MIC=24.4 µM), Listeria monocytogenes ATCC 35152 (MIC=5.7 µM), Micrococcus luteus ATCC 9341 (MIC=20.3 µM), Enterococcus faecalis ATCC 14508 (MIC=57.1 µM), Nocardia asteroides ATCC 3308 (MIC>70 µM), Staphylococcus aureus ATCC 14458 (MIC>70 µM);
    • Fungi: Neurospora crassa FGSC 2489 (IC50=2 µM), Botrytis cinerea ATCC 28387 (IC50=3.1 µM), Fusarium culmorum ATCC 32973 (IC50=0.2 µM).

• • Hemolytic Activity

  • • [Ref.22115565]3.5% hemolytic activity at 6 μM, 11.2% hemolytic activity at 10 μM, 22.5% hemolytic activity at 30 μM, 33.9% hemolytic activity at 50 μM against human red blood cells

• • Cytotoxicity

  • • Not included yet

• • 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 (predict)

• • Structure Description

  • The secondary structure prediction for BmKbpp reveals that BmKbpp is composed of an α-helical structure from amino residues 3-35, followed by a coil-coiled region of three residues (NGP), and ended with an α-helical region of 9 residues (ref.2).

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP03748.

DRAMP03748

• • Function

  • Amphipathic peptide that shows bradykinin potentiating activity and antimicrobial activities against bacteria and fungi. Has higher antibacterial activities against Gram-negative than against Gram-positive bacteria. Also inhibits NADPH oxidase-dependent superoxide production (IC50 is 0.4 µM on granulocytes stimulated with PMA, IC50 is 0.51 µM on HL-60 cells undifferentiated and IC50 is 0.53 µM on HL-60 cells treated with DMSO). The C-terminal peptide shows a higher bradykinin potentiating activity than the complete peptide.

• • Tissue specificity

  • Expressed by the venom gland.

• • Miscellaneous

  • Shows hemolytic activity. Shows a alpha-helical structure. The genomic DNA coding for this protein is not a continuous sequence in the genome. The transcript of this protein may be generated by trans-splicing, by which exons from two independently transcribed pre-mRNAs are joined to form a single mature transcript.

• ·Literature 1

• • Title

  • Cloning and characterization of a novel cDNA sequence encoding the precursor of a novel venom peptide (BmKbpp) related to a bradykinin-potentiating peptide from Chinese scorpion Buthus martensii Karsch.

• • Pubmed ID

  • 10868911

• • Reference

  • IUBMB Life. 2000 Mar;49(3):207-210.

• • Author

  • Zeng XC, Li WX, Peng F, Zhu ZH.

• ·Literature 2

• • Title

  • Characterization of BmKbpp, a multifunctional peptide from the Chinese scorpion Mesobuthus martensii Karsch: gaining insight into a new mechanism for the functional diversification of scorpion venom peptides.

• • Pubmed ID

  • 22115565

• • Reference

  • Peptides. 2012 Jan;33(1):44-51.

• • Author

  • Zeng XC, Wang S, Nie Y, Zhang L, Luo X.