Synthesis of bis N-heterocyclic carbenes,derivatives and metal complexes

A method for the synthesis and isolation of 1,1′-methylene-bis-(3-aryl-imidazol-2-ylidene) ligands, aryl = 2,6-diisopropyl-phenyl (DiPP), L^DiPP, mesityl (mes), L^mes, is reported, which provides synthetically useful quantities of high purity. Derivatisation of L^DiPP with chalcogenides gave the adducts L^DiPPE₂, E = S, Se, Te. Reaction of L^DiPP with [Pd(tmeda)Me₂], [Pt(μ-SMe₂)Me₂]₂, [Ir(1,5-COD)(μ-Cl)]₂/KPF₆ and [NiBr₂(dme)] gave [Pd(L^DiPP)Me₂] (1), [Pt(L^DiPP)Me₂] (2), [Ir(L^DiPP)(1,5-COD)](PF₆) (3) and [Ni(L^DiPP)Br₂] (4), respectively. The latter was reduced in the presence of CO to [Ni(L^DiPP)(CO)₂] (5). The structures of L^mes, L^DiPPTe₂, and 1–5 are also reported.     

Synthesis of Substituted Trans-1,6-Dimethylbicyclo[4.3.0]-non-2-enes Using A Claisen Rearrangement of α-(Thioalkoxy) Esters

The Claisen rearrangement of α-(thioalkoxy)-esters provided access to substituted trans-1, 6-dimethylbicyclo[4.3.0]non-2-enes characteristic of the CD rings of the cucurbitanes.     

Preparation of Stereoregular Isotactic Poly(mandelic acid) through Organocatalytic Ring‐Opening Polymerization of a Cyclic O‐Carboxyanhydride

Poly(mandelic acid) (PMA) is an aryl analogue of poly(lactic acid) (PLA) and a biodegradable analogue of polystyrene. The preparation of stereoregular PMA was realized using a pyridine/mandelic acid adduct (Py?MA) as an organocatalyst for the ring‐opening polymerization (ROP) of the cyclic O‐carboxyanhydride (manOCA). Polymers with a narrow polydispersity index and excellent molecular‐weight control were prepared at ambient temperature. These highly isotactic chiral polymers exhibit an enhancement of the glass‐transition temperature (T_g) of 15 °C compared to the racemic polymer, suggesting potential future application as high‐performance commodity and biomedical materials.     

Initiation of Protein Synthesis with Non-Canonical Amino Acids In Vivo

By transplanting identity elements into E. coli tRNA^fMet, we have engineered an orthogonal initiator tRNA (itRNA^Ty2) that is a substrate for Methanocaldococcus jannaschii TyrRS. We demonstrate that itRNA^Ty2 can initiate translation in vivo with aromatic non-canonical amino acids (ncAAs) bearing diverse sidechains. Although the initial system suffered from low yields, deleting redundant copies of tRNA^fMet from the genome afforded an E. coli strain in which the efficiency of non-canonical initiation equals elongation. With this improved system we produced a protein containing two distinct ncAAs at the first and second positions, an initial step towards producing completely unnatural polypeptides in vivo. This work provides a valuable tool to synthetic biology and demonstrates remarkable versatility of the E. coli translational machinery for initiation with ncAAs in vivo.     

Tuning Internal Strain in Metal–Organic Frameworks via Vapor Phase Infiltration for CO2 Reduction

A gas‐phase approach to form Zn coordination sites on metal–organic frameworks (MOFs) by vapor‐phase infiltration (VPI) was developed. Compared to Zn sites synthesized by the solution‐phase method, VPI samples revealed approximately 2.8 % internal strain. Faradaic efficiency towards conversion of CO₂ to CO was enhanced by up to a factor of four, and the initial potential was positively shifted by 200–300 mV. Using element‐specific X‐ray absorption spectroscopy, the local coordination environment of the Zn center was determined to have square‐pyramidal geometry with four Zn?N bonds in the equatorial plane and one Zn‐OH₂ bond in the axial plane. The fine‐tuned internal strain was further supported by monitoring changes in XRD and UV/Visible absorption spectra across a range of infiltration cycles. The ability to use internal strain to increase catalytic activity of MOFs suggests that applying this strategy will enhance intrinsic catalytic capabilities of a variety of porous materials.     

Expanding the Toolbox of Metal–Phenolic Networks via Enzyme‐Mediated Assembly

Functional coatings are of considerable interest because of their fundamental implications for interfacial assembly and promise for numerous applications. Universally adherent materials have recently emerged as versatile functional coatings; however, such coatings are generally limited to catechol, (ortho‐diphenol)‐containing molecules, as building blocks. Here, we report a facile, biofriendly enzyme‐mediated strategy for assembling a wide range of molecules (e.g., 14 representative molecules in this study) that do not natively have catechol moieties, including small molecules, peptides, and proteins, on various surfaces, while preserving the molecule's inherent function, such as catalysis (≈80 % retention of enzymatic activity for trypsin). Assembly is achieved by in situ conversion of monophenols into catechols via tyrosinase, where films form on surfaces via covalent and coordination cross‐linking. The resulting coatings are robust, functional (e.g., in protective coatings, biological imaging, and enzymatic catalysis), and versatile for diverse secondary surface‐confined reactions (e.g., biomineralization, metal ion chelation, and N‐hydroxysuccinimide conjugation).     

Initiation of Protein Synthesis with Non‐Canonical Amino Acids In Vivo

By transplanting identity elements into E. coli tRNA^fMet, we have engineered an orthogonal initiator tRNA (itRNA^Ty2) that is a substrate for Methanocaldococcus jannaschii TyrRS. We demonstrate that itRNA^Ty2 can initiate translation in vivo with aromatic non‐canonical amino acids (ncAAs) bearing diverse sidechains. Although the initial system suffered from low yields, deleting redundant copies of tRNA^fMet from the genome afforded an E. coli strain in which the efficiency of non‐canonical initiation equals elongation. With this improved system we produced a protein containing two distinct ncAAs at the first and second positions, an initial step towards producing completely unnatural polypeptides in vivo. This work provides a valuable tool to synthetic biology and demonstrates remarkable versatility of the E. coli translational machinery for initiation with ncAAs in vivo.     

Polyphenol‐Mediated Assembly of Proteins for Engineering Functional Materials

Functional materials composed of proteins have attracted much interest owing to the inherent and diverse functionality of proteins. However, establishing general techniques for assembling proteins into nanomaterials is challenging owing to the complex physicochemical nature and potential denaturation of proteins. Here, a simple, versatile strategy is introduced to fabricate functional protein assemblies through the interfacial assembly of proteins and polyphenols (e.g., tannic acid) on various substrates (organic, inorganic, and biological). The dominant interactions (hydrogen‐bonding, hydrophobic, and ionic) between the proteins and tannic acid were elucidated; most proteins undergo multiple noncovalent stabilizing interactions with polyphenols, which can be used to engineer responsiveness into the assemblies. The proteins retain their structure and function within the assemblies, thereby enabling their use in various applications (e.g., catalysis, fluorescence imaging, and cell targeting).