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Proton transfer is essential in virtually all biochemical processes, with enzymes facilitating this transfer by optimizing the proximity and orientation of reactants through site‐specific hydrogen bonds. Proton transfer is also crucial in the rate‐determining step for the ring‐opening polymerization of N‐carboxyanhydrides (NCAs), widely used to prepare various peptidomimetic materials. This study utilizes side chain‐assisted strategy to accelerate the rate of chain propagation by using NCAs with tertiary amine pendants. This moiety enables hydrogen bond formation between the incoming NCA and the polymer amino growing end. The tertiary amine side chain of the NCA forms a proton shuttle, via a less constrained transition state, to facilitate the proton transfer process. Moreover, the tertiary amine side chains enable the precipitation of NCA monomers through in situ protonation during the monomer synthesis. This greatly facilitates the synthesis of these unreported monomers, allowing the direct controlled synthesis of tertiary amine‐pendant polypeptoids. This side chain‐promoted polymerization has rarely been reported. Additionally, the tertiary amine side chains, as widely used functional groups, endow the polymers with unique properties including pH‐ and thermo‐responsiveness, tunable pKas, and siRNA transfection capability. The self‐promoted synthesis, facile monomer preparation, and attractive properties make tertiary amine‐pendant polypeptoids promising materials for various applications.
Proton transfer is essential in virtually all biochemical processes, with enzymes facilitating this transfer by optimizing the proximity and orientation of reactants through site‐specific hydrogen bonds. Proton transfer is also crucial in the rate‐determining step for the ring‐opening polymerization of N‐carboxyanhydrides (NCAs), widely used to prepare various peptidomimetic materials. This study utilizes side chain‐assisted strategy to accelerate the rate of chain propagation by using NCAs with tertiary amine pendants. This moiety enables hydrogen bond formation between the incoming NCA and the polymer amino growing end. The tertiary amine side chain of the NCA forms a proton shuttle, via a less constrained transition state, to facilitate the proton transfer process. Moreover, the tertiary amine side chains enable the precipitation of NCA monomers through in situ protonation during the monomer synthesis. This greatly facilitates the synthesis of these unreported monomers, allowing the direct controlled synthesis of tertiary amine‐pendant polypeptoids. This side chain‐promoted polymerization has rarely been reported. Additionally, the tertiary amine side chains, as widely used functional groups, endow the polymers with unique properties including pH‐ and thermo‐responsiveness, tunable pKas, and siRNA transfection capability. The self‐promoted synthesis, facile monomer preparation, and attractive properties make tertiary amine‐pendant polypeptoids promising materials for various applications.
Proton transfer is essential in virtually all biochemical processes, with enzymes facilitating this transfer by optimizing the proximity and orientation of reactants through site‐specific hydrogen bonds. Proton transfer is also crucial in the rate‐determining step for the ring‐opening polymerization of N‐carboxyanhydrides (NCAs), widely used to prepare various peptidomimetic materials. This study utilizes side chain‐assisted strategy to accelerate the rate of chain propagation by using NCAs with tertiary amine pendants. This moiety enables hydrogen bond formation between the incoming NCA and the polymer amino growing end. The tertiary amine side chain of the NCA forms a proton shuttle, via a less constrained transition state, to facilitate the proton transfer process. Moreover, the tertiary amine side chains enable the precipitation of NCA monomers through in situ protonation during the monomer synthesis. This greatly facilitates the synthesis of these unreported monomers, allowing the direct controlled synthesis of tertiary amine‐pendant polypeptoids. This side chain‐promoted polymerization has rarely been reported. Additionally, the tertiary amine side chains, as widely used functional groups, endow the polymers with unique properties including pH‐ and thermo‐responsiveness, tunable pKas, and siRNA transfection capability. The self‐promoted synthesis, facile monomer preparation, and attractive properties make tertiary amine‐pendant polypeptoids promising materials for various applications.
Cytochrome b 562 is a small redox-active heme protein that has served as an important model system for understanding biological electron transfer processes. Here, we present a comprehensive theoretical study of electron transport mechanisms in protein− metal junctions incorporating cytochrome b 562 using a multi-scale computational approach. Employing molecular dynamics (MD) simulations, we generated junction geometries for both vacuum-dried and solvated conditions, with the protein covalently bound to gold contacts in various configurations. Coherent tunneling, described by the Landauer− Buttiker formalism within the density functional theory (DFT) framework, is compared to the incoherent hopping charge transport mechanism captured by the semi-classical Marcus theory. The tunneling was identified as the dominant mechanism explaining the experimental data measured on the cytochrome b 562 junctions, exhibiting exponential yet very shallow distance dependence. While the structural orientations and protein contacts with the electrodes influence the junction conductance significantly, the solvation effects are relatively small, affecting the electronic properties mostly via the adsorption arrangement. On the other hand, the considerable temperature dependence of the conductance was found strong only for hopping, while the tunneling current magnitudes remain practically unaffected and are a good indicator of the coherent mechanism in this case.
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