Ipsen has filed a patent for a modified botulinum neurotoxin A (BoNT/A) L-chain protease that has enhanced cleavage of human SNAP-23 (hSNAP-23) compared to the unmodified version. The modified protease has a specific amino acid sequence that allows it to bind to the I198 binding site of hSNAP-23 more effectively. GlobalData’s report on Ipsen gives a 360-degree view of the company including its patenting strategy. Buy the report here.

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According to GlobalData’s company profile on Ipsen, Cancer treatment biomarkers was a key innovation area identified from patents. Ipsen's grant share as of September 2023 was 47%. Grant share is based on the ratio of number of grants to total number of patents.

Modified botulinum neurotoxin a (bont/a) l-chain protease for enhanced cleavage of hsnap-23

Source: United States Patent and Trademark Office (USPTO). Credit: Ipsen SA

A recently filed patent (Publication Number: US20230312661A1) describes a modified version of the botulinum neurotoxin A (BoNT/A) L-chain protease. This modified protease has an altered amino acid sequence compared to the wild-type BoNT/A L-chain and demonstrates increased cleavage of human SNAP-23 (hSNAP-23).

The modified BoNT/A L-chain protease includes at least one amino acid residue change within a binding pocket that interacts with the I198 binding site of hSNAP-23. This binding pocket is defined by the amino acid residue K166 of the wild-type BoNT/A L-chain. The modified protease can have amino acid residues such as valine, phenylalanine, leucine, or isoleucine at the position corresponding to K166 of the wild-type L-chain.

Additionally, the modified BoNT/A L-chain protease can have an amino acid residue change within a binding pocket that interacts with the D189/D192 binding site of hSNAP-23. This binding pocket is defined by the amino acid residue Q29 of the wild-type BoNT/A L-chain. The modified protease can have an alanine residue at the position corresponding to Q29 of the wild-type L-chain.

Furthermore, the modified BoNT/A L-chain protease can have amino acid residue changes within binding pockets that interact with the K185, R186, and K206 binding sites of hSNAP-23. These binding pockets are defined by the amino acid residues G305, S143, and Y251 of the wild-type BoNT/A L-chain, respectively. The modified protease can have amino acid residues such as glutamate and aspartate at the positions corresponding to G305, S143, and Y251 of the wild-type L-chain.

The patent also describes a nucleic acid construct encoding the modified BoNT/A L-chain protease and a delivery vehicle for delivering the modified protease or the nucleic acid construct into a target cell, preferably a non-neuronal target cell. The delivery vehicle includes a targeting moiety that binds the vehicle to the target cell and a translocation peptide that facilitates the entry of the modified protease or nucleic acid construct into the target cell.

A method of cleaving hSNAP-23 is disclosed, which involves contacting hSNAP-23 with the modified BoNT/A L-chain protease or the delivery vehicle. The patent also mentions specific amino acid residue changes, such as phenylalanine at the position corresponding to K166 of the wild-type L-chain, and a S254A substitution relative to the wild-type BoNT/A L-chain.

Overall, this patent presents a modified BoNT/A L-chain protease with enhanced cleavage activity towards hSNAP-23, along with related nucleic acid constructs, delivery vehicles, and methods of cleaving hSNAP-23.

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GlobalData Patent Analytics tracks bibliographic data, legal events data, point in time patent ownerships, and backward and forward citations from global patenting offices. Textual analysis and official patent classifications are used to group patents into key thematic areas and link them to specific companies