General Information
-
DRAMP ID
- DRAMP21223
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Peptide Name
- IsCT-p (Derived from IsCT-P)
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Source
- Synthetic construct
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Family
- Not found
-
Gene
- Not found
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Sequence
- ILKKIWKpIKKLF
-
Sequence Length
- 13
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UniProt Entry
- No entry found
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Protein Existence
- Synthetic form
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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Target Organism
-
- [Ref.16040002] Gram-positive bacteria : Staphylococcus aureus(KCTC 1621)(MIC=1 μM), MRSA (CCARM 3001)(MIC=2 μM), MRSA (CCARM 3543)(MIC=1 μM), Bacillus subtilis(KCTC 3068)(MIC=2 μM), Staphylococcus epidermidis(KCTC 1917)(MIC=1 μM);
- Gram-negative bacteria : Escherichia coli(KCTC 1682)(MIC=2 μM), Pseudomonas aeruginosa(KCTC 1637)(MIC=2 μM), MDRPA (CCARM 2095)(MIC=2 μM), Salmonella typhimurium(KCTC 1926)(MIC=2 μM)
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Hemolytic Activity
-
- [Ref.16040002] 0% hemolysis at 200 μM against human red blood cells
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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
- Linear
-
N-terminal Modification
- Free
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C-terminal Modification
- Amidation
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Nonterminal Modifications and Unusual Amino Acids
- None
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Stereochemistry
- Mixed(D-Pro8)
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Structure
- Random coil
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Structure Description
- This result indicated that D-Pro in the central position of a short a-helical peptide provides more remarkable structural flexibility than L-Pro.
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Helical Wheel Diagram
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PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP21223.
Physicochemical Information
-
Formula
- C80H134N18O12
Absent Amino Acids
- ACDEGHMNPQRSTVY
Common Amino Acids
- K
Mass
- 1655.19
PI
- 10.6
Basic Residues
- 5
Acidic Residues
- 0
Hydrophobic Residues
- 7
Net Charge
- +5
-
Boman Index
- 216
Hydrophobicity
- 0.269
Aliphatic Index
- 150
Half Life
-
- Mammalian:20 hour
- Yeast:30 min
- E.coli:>10 hour
Extinction Coefficient Cystines
- 5500
Absorbance 280nm
- 458.33
Polar Residues
- 0
DRAMP21223
Comments Information
Function
- Antibacterial activity against Gram-positive bacteria and Gram-negative bacteria
Literature Information
- ·Literature 1
-
Title
- The role of the central L- or D-Pro residue on structure and mode of action of a cell-selective alpha-helical IsCT-derived antimicrobial peptide.
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Pubmed ID
- 16040002
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Reference
- Biochem Biophys Res Commun. 2005 Sep 9;334(4):1329-35.
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Author
- Lim SS, Kim Y, Park Y, Kim JI, Park IS, Hahm KS, Shin SY