General Information
-
DRAMP ID
- DRAMP21617
-
Peptide Name
- sDRIM
-
Sequence
- qqrkrkiwsⓚlapⓓgttlvklvagig
-
Sequence Length
- 26
-
Original Sequence
- qqrkrkiwsilaplgttlvklvagig
-
Source
- Synthetic construct
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
-
Comments
- Function: Antibacterial activity against Gram-positive and Gram-negative bacteria.
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Target Organism
-
- [Ref.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC = 128 μg/mL), Enterococcus faecalis (MIC = 64 μg/mL);
- Gram-negative bacteria: Escherichia coli (MIC = 32 μg/mL), Pseudomonas aeruginosa (MIC = 64 μg/mL)
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Hemolytic Activity
-
- [Ref.28921993] It has 13.4%, 18.6%, 25.4%, 33.4%, 42.0%, 46.9%, 42.2% and 47.1% hemolysis against human red blood cells at 5, 7.5, 10, 15, 20, 25, 30 and 40 μg/ml.
-
Cytotoxicity
-
- [Ref.28921993] The toxicity of sDRIM toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM.
Structure Information
-
Linear/Cyclic
- Cyclic (Stapled)
-
N-terminal Modification
- Free
-
C-terminal Modification
- Amidation
-
Special Amino Acid and Stapling Position
- ⓚ (10) and ⓓ (14) are corss-linked by lactam stapling through the polar amide bond of a lactam bridge.
-
Stereochemistry
- D
-
Secondary Structure
- ①Disordered (or unstructured) conformation in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②50% average α-helix content in various membranes environments [57% in POPC; 67% in POPC/P
-
Structure Description
- In the cases of sDRIM and sKFGF, stapling did not induce any conformational change, as these analogues remained just as unstructured.
-
Helical Wheel Diagram
-
Predicted Structure
- There is no predicted structure for DRAMP21617.
Physicochemical Information
-
Formula
- C₁₃₁H₂₂₆N₃₈O₃₁
Absent Amino Acids
- ACDEFGHIKLMNPQRST
Common Amino Acids
- ACDEFGHIK
Mass
- 2829.48
PI
- /
-
Basic Residues
- 0
Acidic Residues
- 0
Hydrophobic Residues
- 0
Hydrophobicity
- /
Polar Residues
- 0
DRAMP21617
Literature Information
- Literature 1
-
Title
- Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties.
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Pubmed ID
- 28921993
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Reference
- J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26.
-
Author
- Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich