A Study on the Optically Active Polymer Poly‐β‐pinene

Poly‐β‐pinene (PBP) was obtained by radiation‐induced polymerization of monomer with γ radiation. The polymerizations were conducted both in vacuum and in the presence of air at different radiation doses up to 1–3 MGy. It was found that the presence of oxygen retards the polymerization rate and reduces the polymer yields and the radiation chemical yield suggesting that the polymerization mechanism involves free radicals. It is shown that PBP can also be obtained in low yields from β‐(‐)pinene polymerization with a free radical initiator. The chemical structures of the PBP radiopolymer and PBP obtained by a free radical initiator were studied by FT‐IR and ¹³C CP‐MAS NMR spectroscopy. The data shows that the PBP obtained have highly ordered structures, which is manifested also by the very high specific optical rotation which is about 3 times that of the starting monomer in the case of the radiopolymer and about 5 times in the case of the PBP prepared with the free radical initiator. In contrast, PBP obtained in high yields by cationic polymerization shows a very low specific optical rotation, much lower than that of the starting monomer and low regularity in chemical structure has been attributed to this polymer by FT‐IR and ¹³C CP‐MAS NMR spectroscopy. It is shown that PBP with high optical activity racemizes over an acidic catalyst.     

A De Novo-Designed Type 3 Copper Protein Tunes Catechol Substrate Recognition and Reactivity

De novo metalloprotein design is a remarkable approach to shape protein scaffolds toward specific functions. Here, we report the design and characterization of Due Rame 1 (DR1), a de novo designed protein housing a di-copper site and mimicking the Type 3 (T3) copper-containing polyphenol oxidases (PPOs). To achieve this goal, we hierarchically designed the first and the second di-metal coordination spheres to engineer the di-copper site into a simple four-helix bundle scaffold. Spectroscopic, thermodynamic, and functional characterization revealed that DR1 recapitulates the T3 copper site, supporting different copper redox states, and being active in the O₂-dependent oxidation of catechols to o-quinones. Careful design of the residues lining the substrate access site endows DR1 with substrate recognition, as revealed by Hammet analysis and computational studies on substituted catechols. This study represents a premier example in the construction of a functional T3 copper site into a designed four-helix bundle protein.