Back to search

Peptide record

TPDB13376

Antibacterial Toxicity standard
23 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.
TPDB13376
Antibacterial Toxicity
Anti-infective peptides Toxicity and safety peptides
AntiBP3 Peptipedia
standard
No
A 23-aa standard natural multi-activity (Antibacterial and Toxicity) peptide sequence curated from AntiBP3 and Peptipedia, with an available 3D structural model.
Sequence
GLKRIFKSGLGKLVKGISAHVAS
Physicochemical Analysis
C108H188N32O27
NDCEQMPTWY
GK
2366.88
11.80
6
0
10
+5
2.53
0.343
118.70
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
0
0.00
3
Residue Composition
number
2
A
1
R
0
N
0
D
0
C
0
E
0
Q
4
G
1
H
2
I
3
L
4
K
0
M
1
F
0
P
3
S
0
T
0
W
0
Y
2
V
Amino Acid Distribution
A: 2 R: 1 N: 0 D: 0 C: 0 E: 0 Q: 0 G: 4 H: 1 I: 2 L: 3 K: 4 M: 0 F: 1 P: 0 S: 3 T: 0 W: 0 Y: 0 V: 2
Chemical Descriptors
23
C108H188N32O27
2366.88
11.80
+5
2.53
0.343
Evidence Records 2 records
Evidence 1 Activity

Activity

0% Hemolysis
Toxicity
31.3 µM
Hemolytic Cytotoxic
0% Hemolysis | 31.3 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
Increases in Hydrophilicity and Charge on the Polar Face of Alyteserin 1c Helix Change its Selectivity towards Gram-Positive Bacteria. | Antibiotics (Basel) | 2019
Evidence 2 Activity

Activity

4% Hemolysis
Toxicity
125 µM
Hemolytic Cytotoxic
4% Hemolysis | 125 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
Increases in Hydrophilicity and Charge on the Polar Face of Alyteserin 1c Helix Change its Selectivity towards Gram-Positive Bacteria. | Antibiotics (Basel) | 2019