Cell-free protein synthesis with technical additives – expanding the parameter space of in vitro gene expression

• Tabea Bartsch,
• Stephan Lütz and
• Katrin Rosenthal

Beilstein J. Org. Chem. 2024, 20, 2242–2253, doi:10.3762/bjoc.20.192

• of the intracellular environment on the function and cellular behavior of proteins are composition, viscosity, and macromolecular crowding [16], these parameters could have a strong impact on the protein synthesis performance using CFPS. For example, the addition of chemical chaperones, such as

Synthesis of lipophilic 1-deoxygalactonojirimycin derivatives as D-galactosidase inhibitors

• Georg Schitter,
• Elisabeth Scheucher,
• Andreas J. Steiner,
• Arnold E. Stütz,
• Martin Thonhofer,
• Chris A. Tarling,
• Stephen G. Withers,
• Jacqueline Wicki,
• Katrin Fantur,
• Eduard Paschke,
• Don J. Mahuran,
• Brigitte A. Rigat,
• Michael Tropak and
• Tanja M. Wrodnigg

Beilstein J. Org. Chem. 2010, 6, No. 21, doi:10.3762/bjoc.6.21

• provided lipophilic 1-deoxygalactonojirimycin derivatives which exhibit inhibitory properties against β-glycosidases from E. coli and Agrobacterium sp. as well as green coffee bean α-galactosidase. In preliminary studies, these compounds also showed potential as chemical chaperones for GM1-gangliosidosis

• related β-galactosidase mutants. Keywords: chemical chaperones; 1-deoxy-D-galactonojirimycin; iminosugars; lipophilic galactosidase inhibitor; N-modified iminosugars; Introduction Iminosugars such as compounds 1–4 (Figure 1) have been shown to be potent glycosidase inhibitors and useful tools for the

• -galactosidase from green coffee beans. However, the Ki values are still in the low µM range and thus, suitable for use as chemical chaperones. Gratifyingly, compounds 20 and 22 exhibited IC50 values of 10.9 µM (Ki = 2.0 µM) and 3.26 µM (Ki = 0.72 µM), respectively, with human lysosomal β-galactosidase. In