• DRAMP ID

    • DRAMP21336
    • Peptide Name

    • RPb (Frogs, amphibians, animals)
    • Source

    • synthetic construct
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • SFLTTVKKLVTNLAAL
    • Sequence Length

    • 16
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Synthetic form
    • Biological Activity

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

      • [Ref.31242693] Gram-positive bacteria:Staphylococcus aureus (MIC=8 μM; MBC=8 μM), MRSA (MIC=16 μM; MBC=32 μM), Enterococcus faecalis (MIC=32 μM; MBC=128 μM);
      • Gram-negative bacteria: Escherichia coli (MIC=16 μM; MBC=16 μM), Pseudomonas aeruginosa (MIC=64 μM; MBC=256 μM);
      • Fungi: Candida albicans (MIC=16 μM; MBC=16 μM)
    • Hemolytic Activity

      • [Ref.31242693] 7% hemolysis at 16 μM, 18% hemolysis at 32 μM, 20% hemolysis at 64 μM, 40% hemolysis at 128 μM, 70% hemolysis at 256 μM, 100% hemolysis at 512 μM on horse erythrocytes.
    • Cytotoxicity

      • [Ref.31242693] RPb only possessed inhibitory effect on the proliferation of H157 with the IC value of 6.856 μM, while showed no inhibitory effect on the proliferation of MCF-7, U251MG, PC-3 and MDA-MB-435s. DETAILED DATA: ①The cell viabillity of NCI-H157 induced by RPb is 98.7%, 102.5%, 96.9%, 98.1%, 38.1%, 9.4% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 100%, 95%, 89.4%, 41.2%, 16.2% and 16.2% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ②The cell viability of MCF-7 induced by RPb is 100.6%, 92.5%, 90%, 99.4%, 36.2% and 11.2% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, , while the cell viability induced by Melittin is 100%, 98.1%, 92.5%, 7.5%, 8.7% and 8.7% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ③The cell viability of U251-MG induced by RPb is 105%, 103.1%, 109.4%, 102.5%, 105.6% and 13.1% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 99.4%, 99.4%, 75.6%, 18.7%, 11.9% and 18.1% at 0.001, 0.01, 0.1, 1, 10, 100 μM.④The cell viability of PC-3 induced by RPa is 108.8%, 103.8%, 118.1%, 125.6%, 116.9% and 68.8% at peptide concentrations of 0.001, 0.01, 0.1, 1, 10, 100 μM, while the cell viability induced by Melittin is 110%, 113.1%, 109.4%, 33.1%, 16.9% and 16.2% at 0.001, 0.01, 0.1, 1, 10, 100 μM. ⑤The cell viability of MDA-MB-435S induced by RPa is 98.1%, 95%, 100.6%, 97.5%, 80.6% and 43.1%, while the cell viability induced by Melittin is 100%, 93.1%, 82.5%, 18.8%, 18.8% and 18.1%.
    • 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

    • 49.6% Helix, 7.6% antiparallel, 0% parallel, 9.8% turn and 33% others in 50% TFE/H2O. ##0.3% Helix, 25.4% antiparallel, 0% parallel, 19.4% turn and 55
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP21336 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP21336.
    • Formula

    • C80H139N19O22
    • Absent Amino Acids

    • CDEGHIMPQRWY
    • Common Amino Acids

    • L
    • Mass

    • 1719.1
    • PI

    • 10
    • Basic Residues

    • 2
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +2
    • Boman Index

    • 551
    • Hydrophobicity

    • 0.988
    • Aliphatic Index

    • 146.25
    • Half Life

      • Mammalian:1.9 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 5

DRAMP21336

    • Function

    • Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria. Antifungal activity against Candida albicans.
  • ·Literature 1
    • Title

    • Bioevaluation of Ranatuerin-2Pb from the Frog Skin Secretion of Rana pipiens and its Truncated Analogues
    • Reference

    • Biomolecules. 2019 Jun 25;9(6):249. doi: 10.3390/biom9060249.
    • Author

    • Zhou, XW; Shi, DN; Zhong, RM; Ye, ZM; Ma, CB; Zhou, M; Xi, XP; Wang, L; Chen, TB; Kwok, HF