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Peptide record

TPDB10171

Antibacterial Toxicity standard
23 amino acids
Basic Information
3D PDB MODEL
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TPDB10171
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
GIGKFLHSAKKFGKAWVGEIMNS
Physicochemical Analysis
C116H181N31O29S1
RDCQPTY
GK
2505.96
10.55
5
1
10
+3
1.87
-0.078
72.17
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
5500
219.48
3
Residue Composition
number
2
A
0
R
1
N
0
D
0
C
1
E
0
Q
4
G
1
H
2
I
1
L
4
K
1
M
2
F
0
P
2
S
0
T
1
W
0
Y
1
V
Amino Acid Distribution
A: 2 R: 0 N: 1 D: 0 C: 0 E: 1 Q: 0 G: 4 H: 1 I: 2 L: 1 K: 4 M: 1 F: 2 P: 0 S: 2 T: 0 W: 1 Y: 0 V: 1
Chemical Descriptors
23
C116H181N31O29S1
2505.96
10.55
+3
1.87
-0.078
Evidence Records 2 records
Evidence 1 Activity

Activity

50% Hemolysis
Toxicity
509 µM
Hemolytic Cytotoxic
50% Hemolysis | 509 | 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

25% Hemolysis
Toxicity
271 µM
Hemolytic Cytotoxic
25% Hemolysis | 271 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides. | Biochemistry | 1997