Peptide record

TPDB26699

Antibacterial Anticancer Toxicity standard
9 amino acids
Basic Information
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber.
TPDB26699
Antibacterial Anticancer Toxicity
Anti-infective peptides Cancer-related peptides Toxicity and safety peptides
Peptipedia
standard
No
A 9-aa standard natural multi-activity (Antibacterial, Anticancer, and Toxicity) peptide sequence curated from Peptipedia, with an available 3D structural model.
Sequence
WRTWRTWRT
Physicochemical Analysis
C63H89N21O13
ANDCEQGHILKMFPSYV
RTW
1348.53
12.70
3
0
3
+3
-2.70
-2.033
0.00
Mammalian: 2.8 hour Yeast: 3 min E.coli: 2 min
16500
1223.55
3
Residue Composition
number
0
A
3
R
0
N
0
D
0
C
0
E
0
Q
0
G
0
H
0
I
0
L
0
K
0
M
0
F
0
P
0
S
3
T
3
W
0
Y
0
V
Amino Acid Distribution
A: 0 R: 3 N: 0 D: 0 C: 0 E: 0 Q: 0 G: 0 H: 0 I: 0 L: 0 K: 0 M: 0 F: 0 P: 0 S: 0 T: 3 W: 3 Y: 0 V: 0
Chemical Descriptors
9
C63H89N21O13
1348.53
12.70
+3
-2.70
-2.033
Evidence Records 3 records
Evidence 1 Activity

Activity

10% Hemolysis
Toxicity
>256 µM
Hemolytic Cytotoxic
10% Hemolysis | >256 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
The design of cell-selective tryptophan and arginine-rich antimicrobial peptides by introducing hydrophilic uncharged residues. | Acta Biomater | 2022
Evidence 2 Activity

Activity

10% Cell death
Toxicity
>256 µM
Cytotoxic
10% Cell death | >256 | µM | target cell: Human embryonic kidney HEK293T cells

Target

Human embryonic kidney HEK293T cells

Source & Reference

NA
DBAASP
The design of cell-selective tryptophan and arginine-rich antimicrobial peptides by introducing hydrophilic uncharged residues. | Acta Biomater | 2022
Evidence 3 Activity

Activity

10% Cell death
Toxicity
>256 µM
Cytotoxic
10% Cell death | >256 | µM | target cell: Intestinal Porcine Epithelial Cells IPEC-J2

Target

Intestinal Porcine Epithelial Cells IPEC-J2

Source & Reference

NA
DBAASP
The design of cell-selective tryptophan and arginine-rich antimicrobial peptides by introducing hydrophilic uncharged residues. | Acta Biomater | 2022