General Information
-
DRAMP ID
- DRAMP29029
-
Peptide Name
- Stripe-based foldamer peptide 1
-
Source
- Synthetic construct
-
Family
- N/A
-
Gene
- N/A
-
Sequence
- KLLKKGGKLLKKGGKLLKKGG
-
Sequence Length
- 21
-
UniProt Entry
- No entry found
-
Protein Existence
- Synthetic form
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram-
-
Target Organism
-
- [Ref.33369262] Gram-positive bacteria: Staphylococcus aureus NBRC13276 (MIC > 50 μM) ;
- Gram-negative bacteria: Escherichia coli DH5α (MIC = 12.5 μM), Pseudomonas aeruginosa NBRC13275 (MIC > 50 μM), multidrug-resistant Pseudomonas aeruginosa ATCCBAA-2111 (MDRP) (MIC > 50 μM)
-
Hemolytic Activity
-
- [Ref.33369262] Peptide 1 showed no hemolytic activity up to a concentration of 100 μM.
-
Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
-
Binding Target
Structure Information
-
Linear/Cyclic
- Linear
-
N-terminal Modification
- Free
-
C-terminal Modification
- Free
-
Nonterminal Modifications and Unusual Amino Acids
- None
-
Stereochemistry
- L
-
Structure
- α-Helix content = 25% in 20 mM phosphate buffered saline (PBS) solution (pH 7.4), with 1% sodium dodecyl sulfate
-
Structure Description
- [Ref.33369262] Conversely, the Gly-substitutde peptide 1 showed weaker spectral intensity than other peptides, which suggests a decrease in helicity.
-
Helical Wheel Diagram
-
PDB ID
- None
-
Predicted Structure
- There is no predicted structure for DRAMP29029.
Physicochemical Information
-
Formula
- C102H194N30O22
Absent Amino Acids
- ACDEFHIMNPQRSTVWY
Common Amino Acids
- K
Mass
- 2192.85
PI
- 10.9
Basic Residues
- 9
Acidic Residues
- 0
Hydrophobic Residues
- 6
Net Charge
- +9
-
Boman Index
- -1479
Hydrophobicity
- -0.7
Aliphatic Index
- 111.43
Half Life
-
- Mammalian:1.3 hour
- Yeast:3 min
- E.coli:2 min
Extinction Coefficient Cystines
- 0
Absorbance 280nm
- 0
Polar Residues
- 6
DRAMP29029
Comments Information
Function
- Antibacterial activity against Gram-negative bacteria.
It is a helical foldmer peptide based on "Stripe" (an AMP manually designed) by substituting Ala (position
- 6, 13 and 20) with Gly. The peptide was less active than Stripe against four bacteria
Literature Information
- ·Literature 1
-
Title
- Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling
-
Pubmed ID
- 33369262
-
Reference
- Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749.
-
Author
- Motoharu Hirano, Chihiro Saito, Chihiro Goto, Hidetomo Yokoo, Ryuji Kawano, Takashi Misawa, Yosuke Demizu