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Peptide record

TPDB14270

Antibacterial Antifungal Hemolysis Toxicity standard
59 amino acids
Basic Information
3D PDB MODEL
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TPDB14270
Antibacterial Antifungal Hemolysis Toxicity
Anti-infective peptides Toxicity and safety peptides
dbAMP DRAMP Peptipedia Antifungipept APD_complete APD_hemolytic Hemolytic2
standard
No
A 59-aa standard natural multi-activity (Antibacterial, Antifungal, Hemolysis, and other sources) peptide sequence curated from dbAMP, DRAMP, Peptipedia, and other sources, with an available 3D structural model.
Sequence
GKCSVLKKVACAAAIAGAVAACGGIDLPCVLAALKAAEGCASCFCEDHCHGVCKDLHLC
Physicochemical Analysis
C244H404N70O72S10
RNQMTWY
A
5790.92
6.89
8
5
27
-0
6.96
0.878
99.49
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
625
10.79
12
Residue Composition
number
13
A
0
R
0
N
3
D
10
C
2
E
0
Q
6
G
3
H
2
I
6
L
5
K
0
M
1
F
1
P
2
S
0
T
0
W
0
Y
5
V
Amino Acid Distribution
A: 13 R: 0 N: 0 D: 3 C: 10 E: 2 Q: 0 G: 6 H: 3 I: 2 L: 6 K: 5 M: 0 F: 1 P: 1 S: 2 T: 0 W: 0 Y: 0 V: 5
Chemical Descriptors
59
C244H404N70O72S10
5790.92
6.89
-0
6.96
0.878
Evidence Records 3 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.
Active against both Gram-positive and -negative bacteria as well as mammalian cells (a toxin). This protein has a unique fold. The 3D structure consists of four alpha-helices (residues 7-24, 32–36, 42–47 and 54–58) connected by three loop regions and stabilized by five disulfide bridges: Cys5-Cys42, Cys13-Cys45, Cys24-Cys31, Cys47-Cys55 and Cys51-Cys61. Inactive dimer forms at pH 8 via deprotonation of His50 and His59. A pH-dependent trigger generates the active monomer form. The oligomerization state of the amoebic protein to form a pore (~0.5 nm) is virtually independent of the protein-to-lipid ratio, it may be assumed that acanthaporin functions by a barrel-stave mechanism in membranes. You can rotate, zoom, and view the 3D structure here in the PDB . Updated 2/2014.
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.
Active against both Gram-positive and -negative bacteria as well as mammalian cells (a toxin). This protein has a unique fold. The 3D structure consists of four alpha-helices (residues 7-24, 32–36, 42–47 and 54–58) connected by three loop regions and stabilized by five disulfide bridges: Cys5-Cys42, Cys13-Cys45, Cys24-Cys31, Cys47-Cys55 and Cys51-Cys61. Inactive dimer forms at pH 8 via deprotonation of His50 and His59. A pH-dependent trigger generates the active monomer form. The oligomerization state of the amoebic protein to form a pore (~0.5 nm) is virtually independent of the protein-to-lipid ratio, it may be assumed that acanthaporin functions by a barrel-stave mechanism in membranes. You can rotate, zoom, and view the 3D structure here in the PDB . Updated 2/2014.
Evidence 3 Hemolysis

Source & Reference

APD_complete APD_hemolytic
APD_complete APD_hemolytic

Other

Source Activity Label Source Definition
Hemolysis
APD_complete APD-derived hemolytic peptide annotation. APD_hemolytic APD hemolytic peptide annotation.