General Information

    • DRAMP ID

    • DRAMP21347

    • Peptide Name

    • 2IH1 (De Novo Synthesis)

    • Source

    • synthetic construct

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • IHHIHHH

    • Sequence Length

    • 7

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Synthetic form

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram-

    • Target Organism

      • [Ref.31199117] Gram-negative Bacteria: Escherichia coli 25922 (MIC>64μM), Escherichia coli UB1005 (MIC>64μM), Escherichia coli K88 (MIC>64μM), Escherichia coli K99 (MIC>64μM), Escherichia coli 078 (MIC>64μM), Escherichia coli 987P (MIC>64μM), Pseudomonas aeruginosa 27853 (MIC>64μM), Pseudomonas aeruginosa PAO1 (MIC>64μM), Salmonella typhimurium 14028 (MIC>64μM), Salmonella typhimurium 7731 (MIC>64μM)

    • Hemolytic Activity

      • [Ref.31199117] 5% hemolysis at 63μM, 8% hemolysis at 128μM against human red blood cells

    • Cytotoxicity

      • [Ref.31199117] ①The cell viability of HEK293T cells induced by 2IH1 is 103.6%, 102.2%, 101.7%, 103.9%, 103.6%, 106.1% and 103.3% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 7.4, while that induced by Melittin is 47.2%, 1.7%, 1.9%, 0.6%, 0.6%, 0.6% and 1.7% at 2, 4, 8, 16, 32, 64 and 128 μM. ②The cell viability of HEK293T cells induced by 2IH1 is 107.9%, 104.5%, 103.4%, 102.5%, 101.1%, 105.6% and 102.0% at peptide concentrations of 2, 4, 8, 16, 32, 64 and 128 μM at pH 6.0, while that induced by Melittin is 43.8%, 3.4%, 3.4%, 0%, 2.2%, 0% and 1.1% at 2, 4, 8, 16, 32, 64 and 128 μM.

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • None

    • Stereochemistry

    • L

    • Structure

    • 18% α-helix in 50% TFE/H2O

    • Structure Description

    • The α-helical coiled coils would show a sequence periodicity of seven residues (heptad repeat), indicated as “abcdefg”, with hydrophobic residues in the “a” and “d” positions “forming the knobs-into-holes packing interactions and providing the energy needed to distort the mechanical-stabilized α-helices”.

    • Helical Wheel Diagram

    • DRAMP21347 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP21347.

Physicochemical Information

    • Formula

    • C42H59N17O8

    • Absent Amino Acids

    • ACDEFGKLMNPQRSTVW

    • Common Amino Acids

    • H

    • Mass

    • 930.04

    • PI

    • 7.16

    • Basic Residues

    • 5

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 2

    • Net Charge

    • +5

    • Boman Index

    • -1346

    • Hydrophobicity

    • -1

    • Aliphatic Index

    • 111.43

    • Half Life

      • Mammalian:20 hour
      • Yeast:30 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 0

DRAMP21347

Comments Information

    • Function

    • Antibacterial activity against Gram-negative bacteria.

Literature Information

  • ·Literature 1

    • Title

    • Highly Stabilized α-Helical Coiled Coils Kill Gram-Negative Bacteria by Multicomplementary Mechanisms under Acidic Condition

    • Reference

    • ACS Appl Mater Interfaces. 2019 Jun 26;11(25):22113-22128. doi: 10.1021/acsami.9b04654. Epub 2019 Jun 14.

    • Author

    • Lai Z, Tan P, Zhu Y, Shao C, Shan A, Li L.