| SYNTHESIS |
Meanwhile, Co. has combined the advantages of classic solid- and solution-phase synthesis of peptides in a new high-speed method. According to Co., classic solution-phase peptide synthesis has an edge in being scalable, but each protocol is specific to a particular peptide. It also requires lots of solvent because intermediates must be isolated between amino acid additions. Classic solid-phase synthesis, on the other hand, involves a generic protocol and therefore is amenable to automation. But it is costly--because of solid supports and side-chain protections--and harder to scale up. Combining the strengths of both methods, Co. has invented a new method in which the peptide is anchored in an organic phase through interactions of its hydrophobic C-terminal and side-chain-protecting groups with the solvent, usually ethyl acetate. After a new amino acid is added, the organic phase is washed with water to remove unreacted amino acid and by-products. The next amino acid is then added to the growing peptide. Further improvements will be realized with automation, Co. says. The new method is highly scalable, he points out: The chemistry for 1 g is the same as for 1 kg. That's important, he emphasizes, because the impurity profile of the product does not change, whether it's gram quantities for preclinical studies or kilogram quantities for clinical trials. Van Dijk can't say by how much this method cuts the cost of goods. "But at the very least," he adds, "manufacturing efficiency and flexibility absolutely will go up." |
| UPDATE | 07.03 |
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