Synthesis and Enzymatic Conversion of Amino Acids Equipped with the Silanetriol Functionality: A Prelude to Silicon Biodiversification

• Published in: ChemistryEurope 2023-11, Vol.1 (3), p.n/a
• Main Authors: Dussart‐Gautheret, Jade, Rivollier, Julie, Simon, Cédric, De Simone, Alessandro, Berthet, Jérôme, Delbaere, Stéphanie, Maruchenko, Régina, Troufflard, Claire, Lesage, Denis, Gimbert, Yves, Lemière, Gilles, Marlière, Philippe, Fensterbank, Louis
• Format: Article
• Language: English
• Subjects: Amino acids; aminotransferases; Biosynthesis; Carbon; Chemical Sciences; cluster compounds; Enzymes; hydrosilylation; Peptides; Proteins; silanetriols; Silicon; Transfer RNA; xenobiology
• ISSN: 2751-4765; 2751-4765
• DOI: 10.1002/ceur.202300058

Synthetic routes are reported for the three analogues of the simplest L‐2‐amino‐dicarboxylic acids, aspartate, glutamate, and aminoadipate, in which the silanetriol group (Si(OH)3) replaces the distal carboxyl group (CO2H). Direct access to the silanetriol amino acids relied either on catalytic hydrosilylation of a terminal alkene using triethoxysilane, or on alkylation of a glycine equivalent anion by triallyl(iodomethyl)silane. In both cases, acid hydrolysis afforded the silanetriol amino acids. These were shown to self‐assemble into siloxane Si‐O clusters as their concentration in water increased in the pH range of 1–12. Such reversible cross‐linking did not prevent silanetriol amino acids from serving as substrates of an aminotransferase enzyme, boding well for their utilization as microbial nutrients to encompass silicon in future stages of metabolism and polypeptide edifices. A silanetriol moiety can be appended to amino acid precursors in a straightforward manner, affording unexplored sila‐analogues of aspartate, aminoadipate, and glutamate. They were engaged in an enzymatic process, which opens up broad perspectives for the biologization of silicon.