Elucidating the role of catalytic amino acid residues in the peptide-mediated silica oligomerization reaction mechanism

• DOI: 10.1039/d1cp04542c
• Publication Date: 2022-01-13T20:01:35Z
• Authors: Stephanie R. Hare; Jim Pfaendtner
• Keywords: Diatoms; 0301 basic medicine; 03 medical and health sciences; Proteins; 02 engineering and technology; Amino Acids; Peptides; Silicon Dioxide; 0210 nano-technology

Understanding the detailed mechanism by which proteins of marine diatoms such as silaffins are able to control morphology silica oligomers has eluded synthetic chemists and materials scientists for decades. In this study, we use DFT calculations determine how individual amino acid residues silaffin catalyze dimerization. The reaction network formation a dimer was explored using several different small molecules, including water, guanidinium ions, methylammonium latter two molecules representing analogs arginine lysine, both known play critical roles in enabling catalytic function naturally occurring protein silaffin. It found that lysine analog selectively lowers energy direct water removal pathway silicate Comparing landscapes mechanisms various catalysts provides evidence role side chains oligmerization silica.