Back to search

Peptide record

TPDB08195

Antibacterial Toxicity standard
16 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.
TPDB08195
Antibacterial Toxicity
Anti-infective peptides Toxicity and safety peptides
AntiBP3 Peptipedia
standard
No
A 16-aa standard natural multi-activity (Antibacterial and Toxicity) peptide sequence curated from AntiBP3 and Peptipedia, with an available 3D structural model.
Sequence
RRLRRLLRRLLRRLRR
Physicochemical Analysis
C96H188N46O17
ANDCEQGHIKMFPSTWYV
R
2258.85
13.35
10
0
6
+10
4.74
-1.387
146.25
Mammalian: 1 hour Yeast: 2 min E.coli: 2 min
0
0.00
0
Residue Composition
number
0
A
10
R
0
N
0
D
0
C
0
E
0
Q
0
G
0
H
0
I
6
L
0
K
0
M
0
F
0
P
0
S
0
T
0
W
0
Y
0
V
Amino Acid Distribution
A: 0 R: 10 N: 0 D: 0 C: 0 E: 0 Q: 0 G: 0 H: 0 I: 0 L: 6 K: 0 M: 0 F: 0 P: 0 S: 0 T: 0 W: 0 Y: 0 V: 0
Chemical Descriptors
16
C96H188N46O17
2258.85
13.35
+10
4.74
-1.387
Evidence Records 2 records
Evidence 1 Activity

Activity

0% Hemolysis
Toxicity
10 µM
Hemolytic Cytotoxic
0% Hemolysis | 10 | µM | target cell: Rat erythrocytes

Target

Rat erythrocytes

Source & Reference

NA
DBAASP
Lipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry. | Biochim Biophys Acta | 2009
Evidence 2 Activity

Activity

32% Hemolysis
Toxicity
50 µM
Hemolytic Cytotoxic
32% Hemolysis | 50 | µM | target cell: Rat erythrocytes

Target

Rat erythrocytes

Source & Reference

NA
DBAASP
Lipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry. | Biochim Biophys Acta | 2009