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Peptide record

TPDB07374

Antibacterial Anticancer Antifungal Toxicity standard
13 amino acids
Basic Information
3D PDB MODEL
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TPDB07374
Antibacterial Anticancer Antifungal Toxicity
Anti-infective peptides Cancer-related peptides Toxicity and safety peptides
AntiBP3 dbAMP DRAMP Peptipedia CancerPPD 2.0 CAFPdb
standard
No
A 13-aa standard natural multi-activity (Antibacterial, Anticancer, Antifungal, and other sources) peptide sequence curated from AntiBP3, dbAMP, DRAMP, and other sources, with an available 3D structural model.
Sequence
AKRIVQRIKDFLR
Physicochemical Analysis
C74H131N25O17
NCEGHMPSTWY
R
1643.01
12.13
5
1
6
+4
3.81
-0.515
120.00
Mammalian: 4.4 hour Yeast: >20 hour E.coli: >10 hour
0
0.00
1
Residue Composition
number
1
A
3
R
0
N
1
D
0
C
0
E
1
Q
0
G
0
H
2
I
1
L
2
K
0
M
1
F
0
P
0
S
0
T
0
W
0
Y
1
V
Amino Acid Distribution
A: 1 R: 3 N: 0 D: 1 C: 0 E: 0 Q: 1 G: 0 H: 0 I: 2 L: 1 K: 2 M: 0 F: 1 P: 0 S: 0 T: 0 W: 0 Y: 0 V: 1
Chemical Descriptors
13
C74H131N25O17
1643.01
12.13
+4
3.81
-0.515
Evidence Records 6 records
Evidence 1 Activity

Activity

MIC
Antibacterial
60 µM

Target

M. luteus

Source & Reference

dbAMP DRAMP

Other

Source Activity Label Source Definition
Antibacterial
dbAMP classified as Antibacterial under the Anti-bacterial function class. DRAMP antibacterial activity supported by MIC records against bacterial target organisms.
active against M. luteus (MIC 60 uM) relative to the WT with an MIC of 22 uM. Warning: other bacteria not tested.
Evidence 2 Activity

Activity

MIC
Antifungal
60 µM

Target

M. luteus

Source & Reference

dbAMP DRAMP CAFPdb

Other

Source Activity Label Source Definition
Antifungal
dbAMP classified under the Anti-fungal function class. DRAMP antifungal activity supported by activity records against fungal target organisms.
active against M. luteus (MIC 60 uM) relative to the WT with an MIC of 22 uM. Warning: other bacteria not tested.
Evidence 3 Activity

Activity

10% Hemolysis
Toxicity
>640 µM
Hemolytic Cytotoxic
10% Hemolysis | >640 | µM | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
Disruption of interactions between hydrophobic residues on nonpolar faces is a key determinant in decreasing hemolysis and increasing antimicrobial activities of α-helical amphipathic peptides. | ChemMedChem | 2013
Evidence 4 Activity

Activity

Toxicity
Hemolytic
NA | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents. | J Pept Sci | 2020
Evidence 5 Activity

Activity

Toxicity
Cytotoxic
NA | target cell: Human Lung Fibroblasts

Target

Human Lung Fibroblasts

Source & Reference

NA
DBAASP
Cationic amphipathic peptide analogs of cathelicidin LL-37 as a probe in the development of antimicrobial/anticancer agents. | J Pept Sci | 2020
Evidence 6 Activity

Activity

Toxicity
Hemolytic
Hemolytic_activity: [Ref.23894079] MHC10>640 µM against human red blood cells

Target

erythrocytes

Source & Reference

NA
DRAMP
ChemMedChem. 2013 Oct 8(10):1638-42. doi: 10.1002/cmdc.201300264.