• • DRAMP ID

  • DRAMP03575

• • Peptide Name

  • LL-37(17-29) (C-terminal fragment of LL-37, LL; Human, mammals, animals)

• • Source

  • Homo sapiens

• • Family

  • Belongs to truncated LL-37.

• • Gene

  • Not found

• • Sequence

  • FKRIVQRIKDFLR

• • Sequence Length

  • 13

• • UniProt Entry

  • P49913

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • [Ref.16637646] Gram-negative bacterium: Escherichia coli K12(MIC=40 μM);
    • Drug-resistant KBv cancer cells (LC50=60 μM), Drug-sensitive KB cancer cells (LC50=57 μM).
    • [Ref.28178190]Gram-positive bacteria: Staphylococcus aureus ATCC 29213 (MIC=16 μM), S. faecalis ATCC 29212 (MIC=32 μM), Bacillus subtilis CMCC 63501 (MIC=16 μM), Staphylococcus epidermidis ATCC 12228 (MIC=8 μM);
    • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=16 μM), Escherichia coli UB 1005 (MIC=16 μM), Pseudomonas aeruginosa ATCC 27853 (MIC=8 μM), Pseudomonas aeruginosa PAO1 (MIC=16 μM), Salmonella typhimurium ATCC 14028 (MIC=32 μM), Salmonella typhimurium ATCC 7731 (MIC=16 μM). [Ref.23894079] Gram-positive bacteria : Staphylococcus aureus (ATCC 29213)(MIC=40 μM);
    • Gram-negative bacteria : Escherichia coli (ATCC 25922)(MIC=5 μM)

• • Hemolytic Activity

  • • [Ref.28161291] HC50>256 μM against human red blood cells. [Ref.23894079] MHC10=160 μM against human red blood cells

• • Cytotoxicity

  • • Not included yet

• • Binding Target

  • Not found

• • 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##Random coil

• • Structure Description

  • Not found

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 2FBS resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP03575.

DRAMP03575

• • Function

  • LL-37(17-29) became slightly less active than the longer ones, indicating that the truncated hydrophobic residues L31 and V32 also play a role in interaction with human cells. Antibacterial activity against the Gram-negative bacteria and Gram-positive bacteria.

• ·Literature 1

• • Title

  • Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region.

• • Pubmed ID

  • 16637646

• • Reference

  • J Am Chem Soc. 2006 May 3;128(17):5776-5785.

• • Author

  • Li X, Li Y, Han H, Miller DW, Wang G.

• ·Literature 2

• • Title

  • High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7.

• • Pubmed ID

  • 28178190

• • Reference

  • Int J Mol Sci. 2017 Feb 6;18(2). pii: E339.

• • Author

  • Tan T, Wu D, Li W, Zheng X, Li W, Shan A.

• ·Literature 3

• • Title

  • LL-37-derived membrane-active FK-13 analogs possessing cell selectivity, anti-biofilm activity and synergy with chloramphenicol and anti-inflammatory activity.

• • Pubmed ID

  • 28161291

• • Reference

  • Biochim Biophys Acta Biomembr. 2017 May;1859(5):722-733.

• • Author

  • Rajasekaran G, Kim EY, Shin SY

• ·Literature 4

• • Title

  • Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides.

• • Pubmed ID

  • 23894079

• • Reference

  • ChemMedChem. 2013 Oct;8(10):1638-42.

• • Author

  • Son M, Lee Y, Hwang H, Hyun S, Yu J