Supplementary Material from Protoenzymes: the case of hyperbranched polyesters
2017-10-16T09:16:41Z (GMT) by
Enzymes are biopolymeric complexes that catalyse biochemical reactions and shape metabolic pathways. Enzymes usually work with small molecule cofactors that actively participate in reaction mechanisms and complex, usually globular, polymeric structures capable of specific substrate binding, encapsulation and orientation. Moreover, the globular structures of enzymes possess cavities with modulated microenvironments, facilitating the progression of reaction(s). The globular structure is assured by long folded protein or RNA strands. Synthesis of such elaborate complexes has proven difficult under prebiotically plausible conditions. We explore here that catalysis may have been performed by alternative polymeric structures, namely, hyperbranched polymers. Hyperbranched polymers are relatively complex structures that can be synthesized under prebiotically plausible conditions; their globular structure is assured by virtue of their architecture rather than folding. In this study, we probe the ability of tertiary amine-bearing hyperbranched polyesters to form hydrophobic pockets as a reaction promoting medium for the Kemp elimination reaction. Our results show that polyesters form upon reaction between glycerol, triethanolamine and organic acid containing hydrophobic groups, adipic and methylsuccinic acid, are capable of increasing the rate of Kemp elimination by a factor of up to three over monomeric triethanolamine.