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Peptide record

TPDB34633

Neurotoxin Toxicity standard
82 amino acids
Basic Information
3D PDB MODEL
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TPDB34633
Neurotoxin Toxicity
Toxicity and safety peptides
Peptipedia
standard
No
A 82-aa standard natural multi-activity (Neurotoxin and Toxicity) peptide sequence curated from Peptipedia, with an available 3D structural model.
Sequence
MKTSVVFVIAGLALLSVVCYASELKEQSSVNEVLSTIFHFEQPEERGCLEFWWKCNPNDDKCCRPKLKCSKLFKLCNFSFGK
Physicochemical Analysis
C424H659N107O118S8
LK
9400.02
7.92
12
9
32
+2
13.49
0.004
80.73
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
12865
136.86
24
Residue Composition
number
3
A
2
R
4
N
2
D
7
C
7
E
2
Q
3
G
1
H
2
I
9
L
9
K
1
M
7
F
3
P
8
S
2
T
2
W
1
Y
7
V
Amino Acid Distribution
A: 3 R: 2 N: 4 D: 2 C: 7 E: 7 Q: 2 G: 3 H: 1 I: 2 L: 9 K: 9 M: 1 F: 7 P: 3 S: 8 T: 2 W: 2 Y: 1 V: 7
Chemical Descriptors
82
C424H659N107O118S8
9400.02
7.92
+2
13.49
0.004
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: This cationic hydrophobic peptide acts on a lot of different channels and has an antimicrobial activity. It blocks mechanosensitive ion channels (also named stretch-activated channels or SACs), without having effect on whole-cell voltage-sensitive currents. It also affects acetylcholine receptors (nAChRs) through interactions with membrane lipids by prolonging the closing time without affecting channel conductance or opening activity (PubMed:34374321). It shows high affinity for lipid bilayers (PubMed:15241420, PubMed:29703751). It acts by partitioning into the membrane and perturbing the interface between the channel and the lipid bilayer without necessarily being in physical contact with the channel. It inhibits atrial fibrillation as well as the membrane motor of outer hair cells at low doses. It also binds to the voltage sensor of voltage-gated potassium channels from the archaebacterium Aeropyrum pernix (KvAP) without affecting channel gating. It also shows a low inhibition on a large spectra of sodium channels (Nav1.1/SCN1A, Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.6/SCN8A, Nav1.7/SCN9A) (IC(50)=7.4-14 uM), and potassium channels Kv11.1/KCNH2 and Kv11.2/KCNH6 (IC(50)=11 uM for both) (PubMed:19955179, PubMed:29703751). It exhibits antimicrobial activities against the Gram-positive bacteria B.subtilis (MIC=0.5 uM), S.aureus (MIC=2-4 uM), and S.epidermidis (MIC=4-8 uM), and Gram-negative bacteria S.typhimurium (MIC=32.64 uM), P.aeruginosa (MIC=8-16 uM), and E.coli (MIC=8-16 uM). {ECO:0000269|PubMed:10779316, ECO:0000269|PubMed:11343101, ECO:0000269|PubMed:15241420, ECO:0000269|PubMed:15287735, ECO:0000269|PubMed:16376854, ECO:0000269|PubMed:16797839, ECO:0000269|PubMed:17384064, ECO:0000269|PubMed:17573432, ECO:0000269|PubMed:19955179, ECO:0000269|PubMed:29703751}.

Target

nicotinic acetylcholine receptor (nAChR) acetylcholine receptor voltage-gated sodium channel (Nav) voltage-gated potassium channel (Kv)

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Grammostola rosea (Chilean rose tarantula) (Grammostola spatulata)
Neurotoxin Ion channel impairing toxin Potassium channel impairing toxin Voltage-gated potassium channel impairing toxin Voltage-gated sodium channel impairing toxin
This cationic hydrophobic peptide acts on a lot of different channels and has an antimicrobial activity. It blocks mechanosensitive ion channels (also named stretch-activated channels or SACs), without having effect on whole-cell voltage-sensitive currents.
M-theraphotoxin-Gr1a (M-TRTX-Gr1a) (GsMTx-4) (GsMTx4) (MTx4) (GsMTx-IV)
spider
Neurotoxin 10 (Hwtx-1) family, 52 (MTx4) subfamily
Evidence at protein level
3D-structure Amidation Antibiotic Antimicrobial Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Lipid-binding Neurotoxin Potassium channel impairing toxin Secreted Signal Toxin Voltage-gated potassium channel impairing toxin Voltage-gated sodium channel impairing toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:10779316}.
Additional Detail Fields 7 fields
3D-structure Amidation Antibiotic Antimicrobial Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Lipid-binding Neurotoxin Potassium channel impairing toxin Secreted Signal Toxin Voltage-gated potassium channel impairing toxin Voltage-gated sodium channel impairing toxin
Neurotoxin Ion channel impairing toxin Potassium channel impairing toxin Voltage-gated potassium channel impairing toxin Voltage-gated sodium channel impairing toxin
Evidence at protein level
Neurotoxin 10 (Hwtx-1) family, 52 (MTx4) subfamily
M-theraphotoxin-Gr1a (M-TRTX-Gr1a) (GsMTx-4) (GsMTx4) (MTx4) (GsMTx-IV)
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:10779316}.
spider