From Toxins Targeting Ligand Gated Ion Channels to Therapeutic Molecules
Abstract
:1. Introduction and Scope of the Review
1.1. To be Poisonous or Not: The Dose Effect
1.2. Toxins as Biological Poisons
1.3. Scope of the Review
2. Toxins Targeting the Ligand Gated Ion Channels
2.1. Nicotinic Acetylcholine Receptors
Name | Conus specie | Target | References |
---|---|---|---|
GI, GIA, GII | geographus | Muscle nAChR | [27] |
MI | magus | Muscle nAChR | [28] |
SI, SIA and SII | striatus | Selectivity for the distinct interfaces (α/γ or α/δ) of the muscle-type nAChR | [28,29] |
ImI, ImII | imperialis | Selective for α7 nAChR but also effective on α3β4, α3β2 | [30] |
BuIA | bullatus | Highest potency for α3- and α6−containing nAChRs | [31] |
CnIA, CnIB | consors | Muscle nAChR | [32] |
Ac1.1a, Ac1.1b | achatinus | Muscle nAChR | [33] |
EI | ermineus | Selective for muscle nAChR, also effective on α3β4, α4β2 | [34] |
PnIB, (A10L)-PnIA | pennaceus | Selective for α7, α3β4, α3β2 nAChR | [35,36] |
GIC | geographus | Selective for α3β2 | [37] |
MII | magnus | Selective for α3β2, α3β2β3, α6* nAChR | [38,39] |
PIA | purpurascens | Selective for α6β2, α6β4, α6α3β2(β3), α6α3β4 | [40] |
PIB | purpurascens | Muscle nAChR | [41] |
GID | geographus | α7, α3β2, α4β2 | [42,43] |
AuIA, AuIB and AuIC | aulicus | Selectively blocks α3β4 nAChRs | [44] |
EPI | episcopatus | Selective for α7, α3β2, α3β4 | [45,46] |
AnIB | anemone | α7, α3β2 | [47] |
Vc1.1 | victoriae | α9, α3β4, α3(α5)β2 | [48,49] |
ArIA, ArIB | arenatus | α7, α3β2α6α3β2β3 | [50] |
PeIA | pergrandis | α9α10,α6α3β2β3,α3β2 | [51] |
OmIA | omaria | α7, α3β2 | [52] |
TxIA | textile | α3β2 | [53] |
Lp1.1 | leopardus | α3β2,α6α3β2 | [54] |
SrIA, SrIB | spurious | α4β2, muscle type nAChRs | [55] |
2.2. GABA-A Receptors
2.3. Glycine Receptors
2.4. Serotonin Receptors
2.5. NMDA Receptors
2.6. AMPA Receptors
2.7. Kainate Receptors
2.8. P2X Receptors
3. Current and Proposed Medical Use of Toxins Targeting the LGIC
3.1. nAChR
3.1.1. Agonists
3.1.2. Competitive Antagonists
3.1.3. Non-Competitive Antagonists
3.2. Other Pentameric Ligand Gated Ion Channels
3.3. NMDA Receptors
3.4. AMPA Receptors
3.5. Kainate Receptors
3.6. P2X
4. Conclusion
Appendix: List of Toxins Targeting the LGIC
1. Nicotinic Acetylcholine Receptors
1.1. Peptides and Proteins
1.1.1. Conotoxins
Name | Conus Specie | Target | References |
---|---|---|---|
GI, GIA, GII | geographus | Muscle nAChR | [27] |
MI | magus | Muscle nAChR | [28] |
SI, SIA and SII | striatus | Selectivity for the distinct interfaces (α/γ or α/δ) of the muscle-type nAChR | [28,29] |
ImI, ImII | imperialis | Selective for α7 nAChR but also effective on α3β4, α3β2 | [30] |
BuIA | bullatus | Highest potency for α3- and α6−containing nAChRs | [31] |
CnIA, CnIB | consors | Muscle nAChR | [32] |
Ac1.1a, Ac1.1b | achatinus | Muscle nAChR | [33] |
EI | ermineus | Selective for muscle nAChR, also effective on α3β4, α4β2 | [34] |
PnIB, (A10L)-PnIA | pennaceus | Selective for α7, α3β4, α3β2 nAChR | [35,36] |
GIC | geographus | Selective for α3β2 | [37] |
MII | magnus | Selective for α3β2, α3β2β3, α6∗ nAChR | [38,39] |
PIA | purpurascens | Selective for α6β2, α6β4, α6α3β2(β3), α6α3β4 | [40] |
PIB | purpurascens | Muscle nAChR | [41] |
GID | geographus | α7, α3β2, α4β2 | [42,43] |
AuIA, AuIB and AuIC | aulicus | Selectively blocks α3β4 nAChRs | [44] |
EPI | episcopatus | Selective for α7, α3β2, α3β4 | [45,46] |
AnIB | anemone | α7, α3β2 | [47] |
Vc1.1 | victoriae | α9, α3β4, α3(α5)β2 | [48,49] |
ArIA, ArIB | arenatus | α7, α3β2, α6α3β2β3 | [50] |
PeIA | pergrandis | α9α10,α6α3β2β3,α3β2 | [51] |
OmIA | omaria | α7, α3β2 | [52] |
TxIA | textile | α3β2 | [53] |
Lp1.1 | leopardus | α3β2,α6α3β2 | [54] |
SrIA, SrIB | spurious | α4β2, muscle type nAChRs | [55] |
1.1.2. Snake Neurotoxins
Name | Source | Target | Structural Group | References |
---|---|---|---|---|
α-Bungarotoxin | Bungarus multicinctus | Muscle, α7. | Long-chain α-neurotoxin | [128,129] |
NmmI | Naja mossambica mossambica | Muscle | short-chain α-neurotoxin | [130] |
κ−bungarotoxins | Bungarus genus | α3β2 and other β2-containing nAChRs. | long-chain neurotoxin | [131] |
α-cobratoxin | Naja genus (e.g., Naja kaouthia) | Muscle, α7 | long-chain α-neurotoxins | [132] |
Erabutoxin-a. | Laticauda semifasciata | Muscle | Short-chain α-toxin | |
erabutoxin-b | Laticauda semifasciata | Muscle | short-chain neurotoxin | [133] |
Toxin-α | Naja nigricollis | Muscle | short-chain α-neurotoxin |
1.1.3. Natural Toxic Peptides from Other Species
Name | Origin | Target | Other specifications | References |
---|---|---|---|---|
Candoxin | Bungarus candidus | α7 and muscle. | [ 139] | |
CM-11, CM-2 | Naja haje haje (Egyptian cobra) | Muscle | [ 140] | |
CM10, CM12, CM-13b, CM-14 | Naja haje annulifera | Neuromuscular Junction | [ 141] | |
Cm-9a | N. kaouthia | |||
S4C11 | N. melanoleucaI. | neurotoxin Homologue | [ 142] | |
S5C1, S5C10 | Dendroaspis jamesoni kaimosae (Eastern Jameson's mamba) | Muscle | [ 143] | |
S6C4 | Dendroaspis jamesoni Kaimosae (jameson’s mamba) | 67% sequence identity with Bucandin. | ||
γ-bungarotoxin | Bungarus multicinctus | post synaptic action | [ 144] | |
WTX | Naja kaouthia | α7 and muscle. | [ 138] | |
Wntx-5 | Naja sputatrix | Torpedo α1βγδ, chick α7 | [ 145] | |
NNA2 | the Taiwan cobra (N. n. atra) | Muscle | long-neurotoxin homologue | [ 146] |
LSIII | Laticauda Semifasciata | neuromuscular blockade | [ 147] |
1.2. Alkaloids
1.3. Others
2. GABA-A Receptors
3. Glycine Receptors
4. Serotonin Receptors
5. NMDA
6. AMPA
7. Kainate Receptors
8. P2X Receptors
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Nasiripourdori, A.; Taly, V.; Grutter, T.; Taly, A. From Toxins Targeting Ligand Gated Ion Channels to Therapeutic Molecules. Toxins 2011, 3, 260-293. https://doi.org/10.3390/toxins3030260
Nasiripourdori A, Taly V, Grutter T, Taly A. From Toxins Targeting Ligand Gated Ion Channels to Therapeutic Molecules. Toxins. 2011; 3(3):260-293. https://doi.org/10.3390/toxins3030260
Chicago/Turabian StyleNasiripourdori, Adak, Valérie Taly, Thomas Grutter, and Antoine Taly. 2011. "From Toxins Targeting Ligand Gated Ion Channels to Therapeutic Molecules" Toxins 3, no. 3: 260-293. https://doi.org/10.3390/toxins3030260