• • DRAMP ID

  • DRAMP29092

• • Peptide Name

  • Hn-Mc (a chimeric peptide comprised of the N-terminus of HPA3NT3 and the C-terminus of melittin)

• • Source

  • Synthetic construct

• • Family

  • Not found

• • Gene

  • N/A

• • Sequence

  • FKRLKKLISWIKRKRQQ

• • Sequence Length

  • 17

• • UniProt Entry

  • No entry found

• • Protein Existence

  • Synthetic construct

• • Biological Activity

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

• • Target Organism

  • • [Ref.32731574]Yeast: C. albicans (MIC = 16 μM), C. krusei (MIC = 8 μM), C. parapsilosis (MIC = 16 μM), C. tropicalis (MIC = 4 μM), T. beigellii (MIC = 1 μM);
    • Mold: T. rubrum (MIC = 1-2 μM), F. moniliforme(MIC = 1-2 μM), F. solani(MIC = 1 μM), F. oxysporum(MIC = 1-2 μM), A. flavus(MIC = 2-4 μM), A. fumigatus(MIC = 2-4 μM).
    • [Ref.26028561] Drug-susceptible gram-negative bacteria: E. coli (MIC = 1 μM), P. aeruginosa (MIC = 2 μM);
    • Drug-susceptible gram-positive bacteria: S. aureus (MIC = 2 μM), B. subtilis(MIC = 2 μM);
    • Drug-resistant bacteria: P. aeruginosa DRPA-001 (MIC = 1 μM), P. aeruginosa DRPA-002 (MIC = 1 μM), P. aeruginosa DRPA-003 (MIC = 1 μM), P. aeruginosa DRPA-004 (MIC = 1 μM), P. aeruginosa DRPA-005 (MIC = 2 μM), S. aureus DRSA-001 (MIC = 2 μM), S. aureus DRSA-002 (MIC = 2 μM), S. aureus DRSA-003 (MIC = 1 μM), S. aureus DRSA-004 (MIC = 2 μM), S. aureus DRSA-005 (MIC = 2 μM).

• • Hemolytic Activity

  • • [Ref.26028561] HPA3NT3 and melittin revealed the hemolysis of 68.2% and 100% at 250 μM, respectively, but Hn-Mc was 1.1% at the same concentration

• • Cytotoxicity

  • • [Ref.26028561] The IC50 of HPA3NT3, melittin and Hn-Mc against HaCaT cells were 49.5, 2.8 and 357.5 μM, respectively

• • Binding Target

  • Mitochondria (possibily)

• • Linear/Cyclic

  • Linear

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Amidation

• • Nonterminal Modifications and Unusual Amino Acids

  • None

• • Stereochemistry

  • L

• • Structure

  • Random coil or α-helical structure

• • Structure Description

  • Hn-Mc adopted a random coil structure in the SUVs containing a mammalian membrane and in the buffer; however, it adopted an α-helical structure in SUVs containing a fungal membrane, indicating that it was not bound to the mammalian membrane but rather adhered to or inserted in the fungal membrane. 

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP29092.

DRAMP29092

• • Comment

  • Hn-Mc has a high affinity for the fungal plasma membrane and induces apoptosis in fungal cells, and provide guidance for the development of new antifungal agents. Hn-Mc is an excellent model peptide with potent antibacterial activity and non-cytotoxicity.

• ·Literature 1

• • Title

  • Antifungal Effect of A Chimeric Peptide Hn-Mc against Pathogenic Fungal Strains.

• • Pubmed ID

  • 32731574

• • Reference

  • Antibiotics (Basel). 2020 Jul 28;9(8):454. doi: 10.3390/antibiotics9080454.

• • Author

  • Kim JY, Park SC, Noh G, Kim H, Yoo SH, Kim IR, Lee JR, Jang MK.

• ·Literature 2

• • Title

  • Novel chimeric peptide with enhanced cell specificity and anti-inflammatory activity.

• • Pubmed ID

  • 26028561

• • Reference

  • Biochem Biophys Res Commun. 2015 Jul 31;463(3):322-8. doi: 10.1016/j.bbrc.2015.05.063. Epub 2015 May 29.

• • Author

  • Young-Min Kim, Nam-Hong Kim, Jong-Wan Lee, Jin-Sun Jang, Yung-Hoon Park, Seong-Cheol Park, Mi-Kyeong Jang