General Information
-
DRAMP ID
- DRAMP29006
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Peptide Name
- A4K14-citropin1.1
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Source
- Synthetic construct
-
Family
- N/A
-
Gene
- N/A
-
Sequence
- GLFAVIKKVASVIKGL
-
Sequence Length
- 16
-
UniProt Entry
- No entry found
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Protein Existence
- Synthetic form
Activity Information
-
Biological Activity
- Anticancer
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Target Organism
-
- [Ref.33363118] Cancer cell lines: C4-2B (IC50 = 29.05 μM), A549 (IC50 = 14.97 μM), U87 (IC50 = 14.8 μM), MCF-7 (14.16 μM)
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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
- No cytotoxicity information found in the reference(s) presented
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Binding Target
Structure Information
-
Linear/Cyclic
- Linear
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N-terminal Modification
- Acetylation
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C-terminal Modification
- Amidation
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Nonterminal Modifications and Unusual Amino Acids
- None
-
Stereochemistry
- L
-
Structure
- Helicity = 61.5% in 50% 2,2,2-trifluoroethanol (TFE) aqueous solution (0.1mg/mL)
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Structure Description
- [Ref.33363118] CD analysis indicates that the helicity of intial A4K14-citropin 1.1 was 61.5% and that of the stapled peptides ranged from 13.6 to 89.8%.
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP29006.
Physicochemical Information
-
Formula
- C79H139N19O18
Absent Amino Acids
- CDEHMNPQRTWY
Common Amino Acids
- KV
Mass
- 1643.09
PI
- 10.3
Basic Residues
- 3
Acidic Residues
- 0
Hydrophobic Residues
- 10
Net Charge
- +3
-
Boman Index
- 2023
Hydrophobicity
- 1.394
Aliphatic Index
- 164.38
Half Life
-
- Mammalian:30 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 0
Absorbance 280nm
- 0
Polar Residues
- 3
DRAMP29006
Comments Information
Function
- Antitumor activity against A549, HCT116 and HepG2 cancer cells.
A4K14-citropin 1.1 is a structurally optimized derivative of citropin-1.1 derived from amphibians' skin secreta peptide Citropin, which exhibits broad biological activities. Citropin-1.1 is Amphibian defense peptide with antibiotic and antimicrobial activity. Bowie and his team found that replacement of Asp4 and Gly14 with Ala and Lys (termed A4K14-CITROPIN 1.1) resulted in a more stable α-helix than Citropin on the C-terminal section, and it led to better biologicla activities
Literature Information
- ·Literature 1
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Title
- Design, Synthesis, and Antitumor Activities Study of Stapled A4K14-Citropin 1.1 Peptides
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Pubmed ID
- 33363118
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Reference
- Front Chem. 2020 Dec 10;8:616147. doi: 10.3389/fchem.2020.616147. eCollection 2020.
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Author
- Nan Wang, Gang Xie, Chao Liu, Wei Cong, Shipeng He, Yinghua Li, Li Fan, Hong-Gang Hu