AA sequence: GVRDAYIADDKNCVYTCASNGYCNTECTKNGAESGYCQWIGRYGNACWCIKLPDEVPIRIPGKCR-NH2
Disulfide bonds: C13-C64 ; C17-C37 ; C23-C47 ; C27-C49
Length (aa): 65
Formula: C308H466N90O95S8
Appearance: White lyophilized solid
CAS number: Not available
Molecular Weight: 7206.20 Da
Source: Synthetic
Counterion: TFA salts
Solubility: Water or saline buffer, 5 mg/mL maximum (recommendation)
Purity: >95%
OD1
100 $ – 840 $
OD1, a potent Nav1.7 channel activator
OD1 is a scorpion peptide that has been isolated initially from the venom of the scorpion Odonthobuthus doriae. OD1 potently inhibits fast inactivation of mammalian channels Nav1.7 (EC50 4.5 nM), Nav1.4 (EC50 10 ± 2 nM) and Nav1.6 (EC50 47 ± 10 nM). OD1 also blocks fast inactivation of the para/tipE insect channel (EC50 80 nM). OD1 weakly affects mammalian Nav1.3 and Nav1.5 (EC50 > 1 μM) and does not affect Nav1.2 and Nav1.8. OD1 induces spontaneous pain when injected in animal in association with our without Veratridine and can be used to test the analgesic effects of Nav1.7 blockers in-vivo.
A, C, Time course of the modulating effect of OD1 #ODX001 (50 nM) on hNav1.7 current. The current was elicited by a 50 ms-depolarizing pulse to -25 mV (estimated V1/2) or to -10 mV from a holding potential of -90 mV. Inter-sweep period was 10 s. Current amplitudes were plotted against time. Black bar indicates toxin application. B, D, Representative recording traces of Nav1.7 current in control condition (black) and after the effect of OD1 #ODX001 had stabilized (red). The inactivation kinetics of current was fitted with the standard mono-exponential function. E, Families of hNav1.7 current traces in control and in the presence of 50 nM OD1 #ODX001. Currents were evoked by depolarizing pulses from -60 mV to 40 mV, while the cell was hold at -90 mV. F, Amplitude-voltage relationships obtained from E.
Recently quoted- β-pompilitoxin: sodium channels activator
- ProTx-I: sodium channels blocker
- ProTx-II: Nav1.7 potent blocker
- Biotin-ProTx-II: biotinylated ProTx-II
- Cy5-ProTx-II: fluorescent ProTx-II
- ProTx-III: Nav1.7 selective blocker
- BDS-1: Nav1.7 activator, Kv3.4 blocker
OD1, the first toxin isolated from the venom of the scorpion
Odonthobuthus doriae
In this study, we isolated and pharmacologically characterized the first alpha-like toxin from the venom of the scarcely studied Iranian scorpion Odonthobuthus doriae. The toxin was termed OD1 and its primary sequence was determined: GVRDAYIADDKNCVYTCASNGYCNTECTKNGAESGYCQWIGRYGNACWCIKLPDEVPIRIPGKCR. Using the two-electrode voltage clamp technique, the pharmacological effects of OD1 were studied on three cloned voltage-gated Na+ channels expressed in Xenopus laevis oocytes (Na(v)1.2/beta1, Na(v)1.5/beta1, para/tipE). The inactivation process of the insect channel, para/tipE, was severely hampered by 200 nM of OD1 (EC50 = 80+/-14 nM) while Na(v)1.2/beta1 still was not affected at concentrations up to 5 microM. Na(v)1.5/beta1 was influenced at micromolar concentrations.
Jalali A., et al. (2005) OD1, the first toxin isolated from the venom of the scorpion Odonthobuthus doriae active on voltage-gated Na+ channels. FEBS. PMID: 16038905
Potent Modulation of the Voltage-Gated Sodium Channel Nav1.7 by OD1
Voltage-gated sodium channels are essential for the propagation of action potentials in nociceptive neurons. Nav1.7 is found in peripheral sensory and sympathetic neurons and involved in short-term and inflammatory pain. Nav1.8 and Nav1.3 are major players in nociception and neuropathic pain, respectively. In our effort to identify isoform-specific and high-affinity ligands for these channels, we investigated the effects of OD1, a scorpion toxin isolated from the venom of the scorpion Odonthobuthus doriae. Nav1.3, Nav1.7, and Nav1.8 channels were coexpressed with beta1-subunits in Xenopus laevis oocytes. Na+ currents were recorded with the two-electrode voltage-clamp technique. OD1 modulates Nav1.7 at low nanomolar concentrations: 1) fast inactivation is dramatically impaired, with an EC50 value of 4.5 nM; 2) OD1 substantially increases the peak current at all voltages; and 3) OD1 induces a substantial persistent current. Nav1.8 was not affected by concentrations up to 2 microM, whereas Nav1.3 was sensitive only to concentrations higher than 100 nM. OD1 impairs the inactivation process of Nav1.3 with an EC50 value of 1127 nM. Finally, the effects of OD1 were compared with a classic alpha-toxin, AahII from Androctonus australis Hector and a classic alpha-like toxin, BmK M1 from Buthus martensii Karsch. At a concentration of 50 nM, both toxins affected Nav1.7. Nav1.3 was sensitive to AahII but not to BmK M1, whereas Nav1.8 was affected by neither toxin. In conclusion, the present study shows that the scorpion toxin OD1 is a potent modulator of Nav1.7, with a unique selectivity pattern.
Maertens C., et al. (2006) Potent Modulation of the Voltage-Gated Sodium Channel Nav1.7 by OD1, a Toxin from the Scorpion Odonthobuthus doriae. Mol. Pharmacol. PMID: 16641312
Chemical Engineering and Structural and Pharmacological Characterization of the α‑Scorpion Toxin OD1
Durek T., et al. (2013) Chemical Engineering and Structural and Pharmacological Characterization of the α‑Scorpion Toxin OD1. ACS. PIMD: 3527544