General Information
-
DRAMP ID
- DRAMP29033
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Peptide Name
- Stripe-based foldamer peptide 5
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Sequence
- KLLKKⓏGKLLKKⓍGKLLKKAG
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Sequence Length
- 21
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Original Sequence
- KLLKKAGKLLKKAGKLLKKAG
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Source
- Synthetic construct
Activity Information
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Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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Comments
- Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. It is a helical foldmer peptide based on "Stripe" (an AMP manually designed) by introducing a hydrocarbon stapling. The peptide showed weaker activity than Stripe.
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Target Organism
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- [Ref.33369262] Gram-positive bacteria: Staphylococcus aureus NBRC13276 (MIC = 25 μM) ;
- Gram-negative bacteria: Escherichia coli DH5α (MIC = 6.25 μM), Pseudomonas aeruginosa NBRC13275 (MIC = 12.5 μM), multidrug-resistant Pseudomonas aeruginosa ATCCBAA-2111 (MDRP) (MIC = 25 μM)
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Hemolytic Activity
-
- [Ref.33369262] It exhibits hemolysis at 1.56 μM agasint human red blood cells.
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Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
Structure Information
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Linear/Cyclic
- Cyclic (Stapled)
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N-terminal Modification
- Free
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C-terminal Modification
- Free
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Special Amino Acid and Stapling Position
- ①The Ⓩ (position: 6) in sequence denotes (R)-(7-octenyl)alanine. ②The Ⓧ (position: 13) in sequence denotes (S)-(4-pentenyl)alanine. ③ Ⓩ (6) and Ⓧ (13) are cross-linked by side-stapling through a undec-4-enyl staple.
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Stereochemistry
- L
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Secondary Structure
- α-Helix content = 34% in 20 mM phosphate buffered saline (PBS) solution (pH 7.4), with 1% sodium dodecyl sulfate
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Structure Description
- [Ref.33369262] As shown in Figure 2, peptides 2, 3, 4 and 5 showed negative maxima at around 208 and 222nm, which suggests that they formed stable α-helical structures, similar to Stripe.
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Helical Wheel Diagram
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Predicted Structure
- There is no predicted structure for DRAMP29033.
Physicochemical Information
-
Formula
- C₁₁₇H₂₁₉N₃₁O₂₁
Absent Amino Acids
- CDEFHIMNPQRSTVWY
Common Amino Acids
- K
Mass
- 2396.18
PI
- /
-
Basic Residues
- 9
Acidic Residues
- 0
Hydrophobic Residues
- 7
Hydrophobicity
- /
Polar Residues
- 3
DRAMP29033
Literature Information
- Literature 1
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Title
- Rational Design of Helix-Stabilized Antimicrobial Peptide Foldamers Containing α,α-Disubstituted Amino Acids or Side-Chain Stapling
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Pubmed ID
- 33369262
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Reference
- Chempluschem. 2020 Dec;85(12):2731-2736. doi: 10.1002/cplu.202000749.
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Author
- Motoharu Hirano, Chihiro Saito, Chihiro Goto, Hidetomo Yokoo, Ryuji Kawano, Takashi Misawa, Yosuke Demizu