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Peptide record

TPDB19323

Antibacterial Antifungal Toxicity modified_plain modified
24 amino acids
Basic Information
3D PDB MODEL
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TPDB19323
Antibacterial Antifungal Toxicity
Anti-infective peptides Toxicity and safety peptides
Peptipedia CAFPdb dbAMP
modified_plain
Yes
A 24-aa modified multi-activity (Antibacterial, Antifungal, and Toxicity) peptide sequence curated from Peptipedia, CAFPdb, and dbAMP, with an available 3D structural model.
Modified, details unspecified
Sequence
FLPLLAGLAANFLPKIFXKITRKX
Physicochemical Analysis
C122H199N29O25
DCEQHMSWYV
L
2472.10
11.73
4
0
13
+4
-2.07
0.742
126.25
Mammalian: 1.1 hour Yeast: 3 min E.coli: 2 min
0
0.00
2
Residue Composition
number
3
A
1
R
1
N
0
D
0
C
0
E
0
Q
1
G
0
H
2
I
5
L
3
K
0
M
3
F
2
P
0
S
1
T
0
W
0
Y
0
V
Amino Acid Distribution
A: 3 R: 1 N: 1 D: 0 C: 0 E: 0 Q: 0 G: 1 H: 0 I: 2 L: 5 K: 3 M: 0 F: 3 P: 2 S: 0 T: 1 W: 0 Y: 0 V: 0
Chemical Descriptors
24
C122H199N29O25
2472.10
11.73
+4
-2.07
0.742
Evidence Records 1 records
Evidence 1 Activity

Activity

100% Hemolysis
Toxicity
5 µM
Hemolytic Cytotoxic
100% Hemolysis | 5 | µM | target cell: Rat erythrocytes

Target

Rat erythrocytes

Source & Reference

NA
DBAASP
Structure-function studies on the amphibian peptide brevinin 1E: translocating the cationic segment from the C-terminal end to a central position favors selective antibacterial activity. | J Pept Res | 2001