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Peptide record

TPDB10174

Antibacterial Toxicity standard
23 amino acids
Basic Information
3D PDB MODEL
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TPDB10174
Antibacterial Toxicity
Anti-infective peptides Toxicity and safety peptides
AntiBP3 dbAMP Peptipedia
standard
No
A 23-aa standard natural multi-activity (Antibacterial and Toxicity) peptide sequence curated from AntiBP3, dbAMP, and Peptipedia, with an available 3D structural model.
Sequence
GLGKFLHSAKRFGKAFVGEAMNS
Physicochemical Analysis
C111H174N32O29S1
DCQIPTWY
G
2452.86
10.83
5
1
10
+3
2.30
-0.091
59.57
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
0
0.00
3
Residue Composition
number
3
A
1
R
1
N
0
D
0
C
1
E
0
Q
4
G
1
H
0
I
2
L
3
K
1
M
3
F
0
P
2
S
0
T
0
W
0
Y
1
V
Amino Acid Distribution
A: 3 R: 1 N: 1 D: 0 C: 0 E: 1 Q: 0 G: 4 H: 1 I: 0 L: 2 K: 3 M: 1 F: 3 P: 0 S: 2 T: 0 W: 0 Y: 0 V: 1
Chemical Descriptors
23
C111H174N32O29S1
2452.86
10.83
+3
2.30
-0.091
Evidence Records 2 records
Evidence 1 Activity

Activity

50% Hemolysis
Toxicity
>1000 µM
Hemolytic Cytotoxic
50% Hemolysis | >1000 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides | FEBS Lett | 1997
Evidence 2 Activity

Activity

12% Hemolysis
Toxicity
150 µM
Hemolytic Cytotoxic
12% Hemolysis | 150 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. | Biochemistry | 1997