General Information
-
DRAMP ID
- DRAMP03357
-
Peptide Name
- Cryptdin related sequence peptide (CRS4C-1a; Rodents, mammals, animals)
-
Source
- Mus musculus (Mouse)
-
Family
- Not found
-
Gene
- Defa-rs2
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Sequence
- LQDAALGWGRRCPQCPRCPSCPSCPRCPRCPRCKCNPK
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Sequence Length
- 38
-
Protein Existence
- Transcript level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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Target Organism
-
- Gram-positive bacteria: Enterococcus faecalis (LC=1.9 µM), Lactobacillus fermentum DSM 20052 (LC=1.1 µM), Strepococcus pyogenes clinical isolate (LC=0.4 µM), Listeria monocytogenes type 1 clinical isolate (LC=1.4 µM);
- Gram-negative bacteria: Escherichia coli strain D21 (LC=2.4 µM), Salmonella typhimurium ATCC 14028 (LC=1.7 µM).
- NOTE: Dimerized peptide was two- to fourfold more potent than monomeric peptide. LC, Lethal concentrations.
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
-
- Not included yet
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Binding Target
- Lipopolysaccharide (LPS)-binding
Structure Information
-
Linear/Cyclic
- Not included yet
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N-terminal Modification
- Not included yet
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C-terminal Modification
- Not included yet
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Nonterminal Modifications and Unusual Amino Acids
- Not included yet
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Stereochemistry
- Not included yet
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Structure
- Not found
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP03357.
Physicochemical Information
-
Formula
- C172H284N62O46S9
Absent Amino Acids
- EFHIMTVY
Common Amino Acids
- C
Mass
- 4245.07
PI
- 9.24
Basic Residues
- 8
Acidic Residues
- 1
Hydrophobic Residues
- 5
Net Charge
- +7
-
Boman Index
- -104.67
Hydrophobicity
- -0.821
Aliphatic Index
- 25.79
Half Life
-
- Mammalian:5.5 hour
- Yeast:3 min
- E.coli:2 min
Extinction Coefficient Cystines
- 6000
Absorbance 280nm
- 162.16
Polar Residues
- 14
DRAMP03357
Comments Information
Function
- Antimicrobial peptide that defense response to Gram-negative bacterium and Gram-positive bacterium.
MOA
- CRS peptides were able to bind LPS and to reduce its immunostimulatory activity, leading to a substantial reduction in cellular activation.
Literature Information
- ·Literature 1
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Title
- Increased diversity of intestinal antimicrobial peptides by covalent dimer formation.
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Pubmed ID
- 15235601
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Reference
- Nat Immunol. 2004 Aug;5(8):836-843.
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Author
- Hornef MW, Pütsep K, Karlsson J, Refai E, Andersson M.