General Information
-
DRAMP ID
- DRAMP31797
-
Peptide Name
- Temporin-La
-
Source
- Temporins family
-
Family
-
Gene
- Not found
-
Sequence
- LLRHVVKILEKYL
-
Sequence Length
- 13
-
UniProt Entry
- Notavailable
-
Protein Existence
- Not found
Activity Information
-
Biological Activity
- Antimicrobial, Anticancer
-
Target Organism
-
- Tumor cells:
Target Organism Activity MEC (24.15Inhibition ratio at 50 µg/ml); HL-7702(L-02) (37.22 Inhibition ratio at 50 µg/ml); A549 (45.62 Inhibition ratio at 50 µg/ml); BGC-823 (48.19 Inhibition ratio at 50 µg/ml); Hep-G2 (50.90 Inhibition ratio at 50 µg/ml); HeLa (52.32 Inhibition ratio at 50 µg/ml); SMMC-7721 (52.77 Inhibition ratio at 50 µg/ml); SW1116 57.62 Inhibition ratio at 50 µg/ml
- Tumor cells:
-
Hemolytic Activity
-
- Showed no hemolytic activity against rabbit erythrocytes and human erythrocytes at 250 µg/ml
-
Cytotoxicity
-
- Showed little effects on the proliferation of the 293T human embryonic kidney cell line, MECs, and human lymphomonocytes at concentrations of less than 50 µg/ml
-
Binding Target
- Not available
Structure Information
-
Linear/Cyclic
- Linear
-
N-terminal Modification
- Free
-
C-terminal Modification
- Free
-
Nonterminal Modifications and Unusual Amino Acids
- None
-
Stereochemistry
- L
-
Structure
- Not found
-
Structure Description
- Not found
-
Helical Wheel Diagram
-
PDB ID
- Notavailable
-
Predicted Structure
- There is no predicted structure for DRAMP31797.
Physicochemical Information
-
Formula
- C78H134N20O17
Absent Amino Acids
- ACDFGMNPQSTW
Common Amino Acids
- L
Mass
- 183828
PI
- 10.24
Basic Residues
- 4
Acidic Residues
- 1
Hydrophobic Residues
- 7
Net Charge
- +3
-
Boman Index
- -495
Hydrophobicity
- 0.6
Aliphatic Index
- 194.62
Half Life
-
- Mammalian:5.5 hour
- Yeast:3 min
- E.coli:2 min
Extinction Coefficient Cystines
- 1490
Absorbance 280nm
- 124.17
Polar Residues
- 1
DRAMP31797
Comments Information
A membrane-disturbing action seems to be the major mechanism for cell death
Literature Information
- ·Literature 1
-
Title
- Designed synthetic analogs of the α-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin αvβ3 homing domain
-
Pubmed ID
- 22641352
-
Reference
- J Pept Sci. 2012 Jul;18(7):476-86.
-
Author
- Diao Y, Han W, Zhao H, Zhu S, Liu X, Feng X, Gu J, Yao C, Liu S, Sun C, Pan F.
