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Peptide record

TPDB12826

Antibacterial Anticancer Antifungal Toxicity standard
14 amino acids
Basic Information
3D PDB MODEL
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TPDB12826
Antibacterial Anticancer Antifungal Toxicity
Anti-infective peptides Cancer-related peptides Toxicity and safety peptides
AntiBP3 Peptipedia CAFPdb dbAMP
standard
No
A 14-aa standard natural multi-activity (Antibacterial, Anticancer, Antifungal, and other sources) peptide sequence curated from AntiBP3, Peptipedia, CAFPdb, and other sources, with an available 3D structural model.
Sequence
KRLFKRLFKYLRRF
Physicochemical Analysis
C96H155N29O16
ANDCEQGHIMPSTWV
R
1971.47
12.42
7
0
7
+7
0.20
-0.800
83.57
Mammalian: 1.3 hour Yeast: 3 min E.coli: 2 min
1490
75.58
1
Residue Composition
number
0
A
4
R
0
N
0
D
0
C
0
E
0
Q
0
G
0
H
0
I
3
L
3
K
0
M
3
F
0
P
0
S
0
T
0
W
1
Y
0
V
Amino Acid Distribution
A: 0 R: 4 N: 0 D: 0 C: 0 E: 0 Q: 0 G: 0 H: 0 I: 0 L: 3 K: 3 M: 0 F: 3 P: 0 S: 0 T: 0 W: 0 Y: 1 V: 0
Chemical Descriptors
14
C96H155N29O16
1971.47
12.42
+7
0.20
-0.800
Evidence Records 3 records
Evidence 1 Activity

Activity

7.66±0.46% Hemolysis
Toxicity
32 µM
Hemolytic Cytotoxic
7.66±0.46% Hemolysis | 32 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
D- and Unnatural Amino Acid Substituted Antimicrobial Peptides With Improved Proteolytic Resistance and Their Proteolytic Degradation Characteristics. | Front Microbiol | 2020
Evidence 2 Activity

Activity

29.58±0.83% Hemolysis
Toxicity
64 µM
Hemolytic Cytotoxic
29.58±0.83% Hemolysis | 64 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
D- and Unnatural Amino Acid Substituted Antimicrobial Peptides With Improved Proteolytic Resistance and Their Proteolytic Degradation Characteristics. | Front Microbiol | 2020
Evidence 3 Activity

Activity

37.14±1.29% Hemolysis
Toxicity
128 µM
Hemolytic Cytotoxic
37.14±1.29% Hemolysis | 128 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
D- and Unnatural Amino Acid Substituted Antimicrobial Peptides With Improved Proteolytic Resistance and Their Proteolytic Degradation Characteristics. | Front Microbiol | 2020