General Information
-
DRAMP ID
- DRAMP03603
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Peptide Name
- Human beta-defensin 28 (hBD-28; hBD28; Human, mammals, animals)
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Source
- Homo sapiens (Human)
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Family
- Belongs to the beta-defensin family
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Gene
- Not found
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Sequence
- ARLKKCFNKVTGYCRKKCKVGERYEIGCLSGKLCCAN
-
Sequence Length
- 37
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UniProt Entry
- No entry found
-
Protein Existence
- Not found
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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Target Organism
-
- Gram-negative bacteria: Escherichia coli DSM1103 (MIC=37.5 µg/ml), Klebsiella pneumoniae DSM681 (MIC=50 µg/ml), Pseudomonas aeruginosa DSM1128 (MIC=37.5 µg/ml);
- Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC=25 µg/ml), Streptococcus pneumoniae DSM11865 (MIC=37.5 µg/ml).
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Hemolytic Activity
-
- [Ref.15625724] It is slightly hemolytic (<12%) against human erythrocytes at the highest concentration of 500 μg/ml.
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Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Cyclic
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N-terminal Modification
- Free
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C-terminal Modification
- Free
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Nonterminal Modifications and Unusual Amino Acids
- Disulfide bonds between Cys6 and Cys34,Cys14 and Cys28,Cys18 and Cys35
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Stereochemistry
- L
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Structure
- Bridge
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Structure Description
- Not found
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Helical Wheel Diagram
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PDB ID
- None
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Predicted Structure
- Please click DRAMP03603_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C178H301N55O48S6
Absent Amino Acids
- DHMPQW
Common Amino Acids
- K
Mass
- 4172.05
PI
- 9.54
Basic Residues
- 10
Acidic Residues
- 2
Hydrophobic Residues
- 9
Net Charge
- +8
-
Boman Index
- -70.96
Hydrophobicity
- -0.4
Aliphatic Index
- 63.24
Half Life
-
- Mammalian:4.4 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 3355
Absorbance 280nm
- 93.19
Polar Residues
- 16
DRAMP03603
Comments Information
Function
- Has antibacterial activity gaginst Gram-positive and the Gram-negative bacteria.
Literature Information
- ·Literature 1
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Title
- Engineering disulfide bonds of the novel human beta-defensins hBD-27 and hBD-28: differences in disulfide formation and biological activity among human beta-defensins.
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Pubmed ID
- 15625724
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Reference
- Biopolymers. 2005;80(1):34-49.
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Author
- Schulz A, Klüver E, Schulz-Maronde S, Adermann K.