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Peptide record

TPDB03569

Antibacterial Anticancer Antifungal Antiparasitic Antiviral standard
44 amino acids
Basic Information
3D PDB MODEL
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TPDB03569
Antibacterial Anticancer Antifungal Antiparasitic Antiviral
Anti-infective peptides Cancer-related peptides
AntiBP3 dbAMP DRAMP Peptipedia AntiCP 2.0 iACP-DRLF Antifungipept
standard
No
A 44-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
QLKKCWNNYVQGHCRKICRVNEVPEALCENGRYCCLNIKELEAC
Physicochemical Analysis
C219H353N67O64S7
DMFST
C
5173.04
7.92
8
5
14
+2
12.78
-0.507
77.50
Mammalian: 0.8 hour Yeast: 10 min E.coli: >10 hour
8855
171.18
16
Residue Composition
number
2
A
3
R
5
N
0
D
7
C
5
E
2
Q
2
G
1
H
2
I
4
L
4
K
0
M
0
F
1
P
0
S
0
T
1
W
2
Y
3
V
Amino Acid Distribution
A: 2 R: 3 N: 5 D: 0 C: 7 E: 5 Q: 2 G: 2 H: 1 I: 2 L: 4 K: 4 M: 0 F: 0 P: 1 S: 0 T: 0 W: 1 Y: 2 V: 3
Chemical Descriptors
44
C219H353N67O64S7
5173.04
7.92
+2
12.78
-0.507
Evidence Records 4 records
Evidence 1 Activity

Activity

Antibacterial

Source & Reference

dbAMP DRAMP

Other

Source Activity Label Source Definition
Antibacterial
dbAMP classified as Antibacterial under the Anti-bacterial function class.
Recombinantly expressed peptide is active against E. coli but not S.aureus and S.cerevisiae. Refer to AP1315 reference for additional activity assays using synthetic hBD-27. Warning: Other bacteria not tested. Also, it was found the synthetic form was inactive against 5 bacteria (MIC100 >300 ug/ml) ( Schulz et al., 2005 ). More studies are needed to clarify its antimicrobial activity. It is proposed that the peptides encoded by DEFB23, DEFB27, and DEFB29 genes exert physiological functions in the male genital tract, which may not be related to bacterial inhibition in host defense ( der Naturwissenschaften, 2003 ).
Evidence 2 Activity

Activity

Antifungal

Source & Reference

dbAMP DRAMP Antifungipept

Other

Source Activity Label Source Definition
Antifungal
dbAMP classified under the Anti-fungal function class.
Recombinantly expressed peptide is active against E. coli but not S.aureus and S.cerevisiae. Refer to AP1315 reference for additional activity assays using synthetic hBD-27. Warning: Other bacteria not tested. Also, it was found the synthetic form was inactive against 5 bacteria (MIC100 >300 ug/ml) ( Schulz et al., 2005 ). More studies are needed to clarify its antimicrobial activity. It is proposed that the peptides encoded by DEFB23, DEFB27, and DEFB29 genes exert physiological functions in the male genital tract, which may not be related to bacterial inhibition in host defense ( der Naturwissenschaften, 2003 ).
Evidence 3 Activity

Activity

Antiparasitic

Source & Reference

DRAMP

Other

Recombinantly expressed peptide is active against E. coli but not S.aureus and S.cerevisiae. Refer to AP1315 reference for additional activity assays using synthetic hBD-27. Warning: Other bacteria not tested. Also, it was found the synthetic form was inactive against 5 bacteria (MIC100 >300 ug/ml) ( Schulz et al., 2005 ). More studies are needed to clarify its antimicrobial activity. It is proposed that the peptides encoded by DEFB23, DEFB27, and DEFB29 genes exert physiological functions in the male genital tract, which may not be related to bacterial inhibition in host defense ( der Naturwissenschaften, 2003 ).
Evidence 4 Activity

Activity

Antiviral

Source & Reference

DRAMP

Other

Recombinantly expressed peptide is active against E. coli but not S.aureus and S.cerevisiae. Refer to AP1315 reference for additional activity assays using synthetic hBD-27. Warning: Other bacteria not tested. Also, it was found the synthetic form was inactive against 5 bacteria (MIC100 >300 ug/ml) ( Schulz et al., 2005 ). More studies are needed to clarify its antimicrobial activity. It is proposed that the peptides encoded by DEFB23, DEFB27, and DEFB29 genes exert physiological functions in the male genital tract, which may not be related to bacterial inhibition in host defense ( der Naturwissenschaften, 2003 ).