• • DRAMP ID

  • DRAMP21463

• • Peptide Name

  • Qa (De Novo Synthesis)

• • Source

  • synthetic construct

• • Family

  • Not found

• • Gene

  • Not found

• • Sequence

  • IHKFWRRWFKHI

• • Sequence Length

  • 12

• • UniProt Entry

  • No entry found

• • Protein Existence

  • Synthetic form

• • Biological Activity

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

• • Target Organism

  • • [Ref.30538681] Gram-positive bacteria:Staphylococcus aureus ATCC 29213(MIC=8μM), Staphylococcus aureus ATCC 43300(MIC=16μM), Staphylococcus epidermidis ATCC 12228(MIC=16μM), Streptococci faecalis ATCC 29212(MIC=16μM), Bacillus subtilis CMCC 63501(MIC=32μM);
    • Gram-negative bacteria:Escherichia coli ATCC 25922(MIC=16μM), Escherichia coli UB 1005(MIC=8μM), bacteria pyocyaneum ATCC 27853(MIC=16μM), Salmonella typhimurium ATCC 7731(MIC=16μM), Salmonella Pulloru C79-13(MIC=16μM)

• • Hemolytic Activity

  • • [Ref.30538681] MHC>128μM against human blood cells.The minimum hemolytic concentration (MHC) is defined as the peptide concentration resulting in 5% hemolysis.

• • Cytotoxicity

  • • [Ref.30538681] The cell viability of intestinal epithelial cells (IPEC-J2) induced by Qa is 61.3%, 66.8%, 76.5%, 71.4%, 72.4%, 73.3%, 65.9% and 39.6% at peptide concentrations of 1, 2, 4, 8, 16, 32, 64 and 128 μM.

• • Binding Target

  • Not found

• • Linear/Cyclic

  • Linear

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Amidation

• • Nonterminal Modifications and Unusual Amino Acids

  • None

• • Stereochemistry

  • L

• • Structure

  • α-helix predicted by I-Tasser

• • Structure Description

  • In PBS, the α-helix content of PQ is 2.89% and the β-strand content of that is 19.89%. In SDS, the α-helix content of PQ is 5.54% and the β-strand of that is 14.12%. In TFE, the α-helix content of PQ is 3.08% and the β-strand of that is 18.1%.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP21463.

DRAMP21463

• • Function

  • Antibacterial activity against Gram-positive bacteria and Gram-nagetive bacteria.

• ·Literature 1

• • Title

  • Short Symmetric-End Antimicrobial Peptides Centered on β-Turn Amino Acids Unit Improve Selectivity and Stability

• • Pubmed ID

  • 30538681

• • Reference

  • Front Microbiol. 2018; 9: 2832. Published online 2018 Nov 27. doi: 10.3389/fmicb.2018.02832

• • Author

  • Na Dong, Shuli Chou, Jiawei Li, Chenyu Xue, Xinran Li, Baojing Cheng, Anshan Shan, and Li Xu