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Peptide record

TPDB27818

CTX Blood-Brain Barrier Cell-penetrating Peptides Neurotoxin Toxicity standard
36 amino acids
Basic Information
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber.
TPDB27818
CTX
Blood-Brain Barrier Cell-penetrating Peptides Neurotoxin Toxicity
Toxicity and safety peptides Delivery and barrier-penetrating peptides
BBPpredict Peptipedia CPPsite3.0 NTxPred2 pep-lab
standard
No
A 36-aa standard natural multi-activity (Blood-Brain Barrier, Cell-penetrating Peptides, Neurotoxin, and other sources) peptide sequence curated from BBPpredict, Peptipedia, CPPsite3.0, and other sources, with an available 3D structural model.
Sequence
MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCR
Physicochemical Analysis
C158H256N52O48S11
NEISWV
C
4004.75
8.10
7
3
7
+3
7.03
-0.547
13.61
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
1990
49.69
13
Residue Composition
number
1
A
3
R
0
N
3
D
8
C
0
E
2
Q
5
G
1
H
0
I
1
L
3
K
3
M
1
F
2
P
0
S
2
T
0
W
1
Y
0
V
Amino Acid Distribution
A: 1 R: 3 N: 0 D: 3 C: 8 E: 0 Q: 2 G: 5 H: 1 I: 0 L: 1 K: 3 M: 3 F: 1 P: 2 S: 0 T: 2 W: 0 Y: 1 V: 0
Chemical Descriptors
36
C158H256N52O48S11
4004.75
8.10
+3
7.03
-0.547
Free
L
Linear
Free
N[C@@H](CCCN=C)C(=O)N[C@@H](CCCN=C)C(=O)N[C@@H](CCCN=C)C(=O)N[C@@H](CCCN=C)C(=O)N[C@@H](CCCN=C)C(=O)N[C@@H](CCCN=C)C(=O)N[C@@H](CCCN=C)C(=O)N[C@@H](CCCN=C)C(=O)N[C@@H](CCCN=C)C(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)O N[C@@H](CCSC)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCSC)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1[nH]cnc1)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCN=C)C(=O)N[C@@H](CCCN=C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)NCC(=O)NCC(=O)N[C@@H](CCCN=C)C(=O)NCC(=O)N[C@@H](CCCN=C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC1=CN=C(C)/C/1=C\C)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCN=C)C(=O)O
Evidence Records 3 records
Evidence 1 Activity

Activity

Cell-penetrating Peptides

Target

HeLa Cells And hCMEC/D3 Cells

Source & Reference

CPPsite3.0
CPPsite3

Other

Source Activity Label Source Definition
Cell-penetrating Peptides
CPPsite3.0 experimentally validated cell-penetrating peptide annotation.
Natural residues Linear L
Protein derived
Alexa Fluor® 488 flourscent dyes
Endosomes
Poor internalization similar extent as TAT-N
Receptor-mediated energy-dependent mechanism
In vitro
CCEETTEECCSSSCSSTTC
Evidence 2 Activity

Activity

Cell-penetrating Peptides

Target

HeLa Cells

Source & Reference

CPPsite3.0
CPPsite3

Other

Natural residues Linear L
Protein derived
Cy5.5™ flourscent dye
Endosomes
Showed an improved ratio of internalization compared to TAT-N
Receptor-mediated energy-dependent mechanism
In vitro
CCCTTCCSSSSSCCSCCTTTTCSBTTTBSSCSSCC
Evidence 3 Activity

Activity

Neurotoxin
FUNCTION: This toxin binds to the surface of glioma cells, and inhibits their proliferation without having effects on normal brain cells. In this context, this toxin has been described as a chloride channel inhibitor (probably ClC-3/CLCN3) by causing its internalization via caveolae (PubMed:16520829). It has also been described to selectively interact with MMP2 (in complex with MT1-MMP (MMP14) and TIMP2), to inhibit its enzymatic activity and to decrease its presence at the cell surface (PubMed:12454020). Additionally, annexin A2 that is expressed on the surface of multiple human tumor cell lines and vascular endothelial cells in culture may be another molecular target, since surface binding of this peptide to the pancreatic tumor cell line Panc-1 is dependent on the expression of annexin A2 using siRNA-mediated specific knockdown of annexin A2 levels (PubMed:20018898). {ECO:0000269|PubMed:12454020, ECO:0000269|PubMed:16520829, ECO:0000269|PubMed:20018898, ECO:0000269|PubMed:8383429}.

Target

voltage-gated calcium channel (Cav)

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) (Deathstalker scorpion)
Neurotoxin Chloride channel impairing toxin Ion channel impairing toxin Voltage-gated chloride channel impairing toxin
This toxin binds to the surface of glioma cells, and inhibits their proliferation without having effects on normal brain cells. In this context, this toxin has been described as a chloride channel inhibitor (probably ClC-3/CLCN3) by causing its internalization via caveolae (PubMed:16520829).
Chlorotoxin (CTX) (ClTx) (Tozuleristide)
scorpion
Short scorpion toxin superfamily, Chloride channel inhibitor family
Evidence at protein level
3D-structure Chloride channel impairing toxin Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Metalloenzyme inhibitor Metalloprotease inhibitor Neurotoxin Protease inhibitor Secreted Toxin Voltage-gated chloride channel impairing toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:8383429}.
Additional Detail Fields 8 fields
CCEETTEECCSSSCSSTTC CCCTTCCSSSSSCCSCCTTTTCSBTTTBSSCSSCC
3D-structure Chloride channel impairing toxin Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Metalloenzyme inhibitor Metalloprotease inhibitor Neurotoxin Protease inhibitor Secreted Toxin Voltage-gated chloride channel impairing toxin
Neurotoxin Chloride channel impairing toxin Ion channel impairing toxin Voltage-gated chloride channel impairing toxin
Evidence at protein level
Short scorpion toxin superfamily, Chloride channel inhibitor family
Chlorotoxin (CTX) (ClTx) (Tozuleristide)
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:8383429}.
scorpion