Small molecule MPD boosts detergent-substitute performance for hybrid catalysis
Congratulations Julia Kinzel on her recent Publication!ACS Publications
Transmembrane proteins have a hydrophobic middle part due to their presence in natural lipid bilayer. Therefore, stabilizing agents are essentially used to cover hydrophobic regions to solubilize purified transmembrane proteins for usage in aqueous media. 2-Methyl-2,4-pentanediol -MPD- a small molecule was applied for stabilization of ferric hydroxamate uptake protein component A, FhuA, which is a transmembrane protein found in the outer membrane of Escherichia coli. The β-barrel shaped protein was used for hosting a rhodium catalyst to perform a polymerization reaction of phenylacetylene as proof of concept. MPD does not form micelles compared to other commonly used detergents such as sodium dodecylsulfate and polyethylene polyethyleneglycol leading to higher polymer product yield and polymer masses. Computer-based simulations supported the suitability of the amphiphilic MPD molecules for successful stabilization of the transmembrane protein FhuA and enabling the functionality of the protein channel.
Access information of this article can be found under Publications and patents and
Kinzel, J., Sauer, D. F., Bocola, M., Arlt, M., Mirzaei Garakani, T., Thiel, A., Beckerle, K., Polen, T., Okuda, J., Schwaneberg, U.; 2-Methyl-2,4-pentanediol (MPD) boosts as detergent-substitute the performance of ß-barrel hybrid catalyst for phenylacetylene polymerization; Beilstein J. Org. Chem. 2017, 13, 1498-1506 [DOI: 10.3762/bjoc.13.148.]