300587-89-7
Chemical Structure
UCB1244283
- CAS No.: 300587-89-7
- Formula:C20H25NO2
- Molecular Weight:311.42
InChIKey: XJYBAKSVSQKCNC-UHFFFAOYSA-N
SMILES: O=C(NC1=CC=CC=C1OC)CC(C)CC2=CC(C)=CC(C)=C2
Biological Activity: UCB1244283 is an SV2A allosteric modulator. UCB1244283 stabilizes the closed SV2A conformation by binding to an intraluminal allosteric site, slows the dissociation of orthosteric ligands, and increases the affinity of Brivaracetam and the capacity of Levetiracetam (HY-B0106), and selectively binds SV2A rather than SV2B/SV2C through Leu655. UCB1244283 exhibits anticonvulsant activity, provides protection against tonic and clonic seizures, and can be used in epilepsy research[1][2][3][4][5][6][7][8].
| Cat. No. | Product Name | Purity | Description | Pricing | |||||||||||||||||||
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UCB1244283 | 99.97% | UCB1244283 is an SV2A allosteric modulator. UCB1244283 stabilizes the closed SV2A conformation by binding to an intraluminal allosteric site, slows the dissociation of orthosteric ligands, and increases the affinity of Brivaracetam and the capacity of Levetiracetam (HY-B0106), and selectively binds SV2A rather than SV2B/SV2C through Leu655. UCB1244283 exhibits anticonvulsant activity, provides protection against tonic and clonic seizures, and can be used in epilepsy research. | ||||||||||||||||||||
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References
- [1]. Pidathala S, et al. Structural pharmacology of SV2A reveals an allosteric modulation mechanism in the major facilitator superfamily. Nature communications. 2025 Nov 28;16(1):10748. [Content Brief]
- [2]. Daniels V, et al. Modulation of the conformational state of the SV2A protein by an allosteric mechanism as evidenced by ligand binding assays. British journal of pharmacology. 2013 Jul;169(5):1091-101.
- [3]. Wood MD, et al. Further evidence for a differential interaction of brivaracetam and levetiracetam with the synaptic vesicle 2A protein. Epilepsia. 2018 Sep;59(9):e147-e151. [Content Brief]
- [4]. Wood MD, et al. Evidence for a differential interaction of brivaracetam and levetiracetam with the synaptic vesicle 2A protein. Epilepsia. 2017 Feb;58(2):255-262.
- [5]. Mittal A, et al. Structures of synaptic vesicle protein 2A and 2B bound to anticonvulsants. Nature structural & molecular biology. 2024 Dec;31(12):1964-1974.
- [6]. Kammerer RA, et al. Molecular insights into anticonvulsant and botulinum neurotoxin binding of synaptic vesicle glycoprotein 2. Trends in neurosciences. 2025 Dec;48(12):1039-1053.
- [7]. Wood M, et al. Pharmacological profile of the novel antiepileptic drug candidate padsevonil: interactions with synaptic vesicle 2 proteins and the GABAA receptor. The Journal of Pharmacology and Experimental Therapeutics. 2020 Jan 1;372(1):1-0. [Content Brief]
- [8]. Mittal A, et al. Mechanisms underlying allosteric modulation of antiseizure medication binding to synaptic vesicle protein 2A (SV2A). Proceedings of the National Academy of Sciences of the United States of America. 2025 Sep 09;122(36):e2510239122.
