Sequence modification in copoly(ester-imide)s: a catalytic/supramolecular approach to the evolution and reading of copolymer sequence information

Catalytic ester-interchange reactions, analogous to mutation and recombination, allow new sequence information to be written statistically into poly(ester-imide) chains based on NDI (1,4,5,8-naphthalenetetracarboxylic diimide) units. Thus, both the insertion of the cyclic ester cyclopentadecanolide (“exaltolide”) into an NDI-based homopolymer and quantitative sequence exchange between two different homopoly(ester-imide)s are catalyzed by di-n-butyl tin(IV) oxide. Emerging sequences are identified at the triplet and quintet levels using supramolecular complexation of pyrene-d10 at the NDI residues to amplify the separation of 1H NMR resonances associated with different sequences. In such systems, pyrene is able to act as a “reader molecule” by generating different levels of ring-current shielding from the different patterns of supramolecular binding to all NDI-centered sequences of a given length.

Sequence-Modification in Copoly(ester-Imide)s: A Catalytic/supramolecular Approach to Writing/reading Copolymer Sequence-Information

Catalytic ester-interchange reactions, analogous to mutation and recombination, allow new sequence-information to be written, statistically, into NDI-based poly(ester-imide) chains. Thus, insertion of the cyclic ester cyclopentadecanolide ("exaltolide") into an NDI-based homopolymer, and quantitative sequence-exchange between two different homopoly(ester-imide)s, are catalysed by di-<i>n</i>-butyl tin(IV) oxide. Emerging sequences are identified at the triplet and quintet levels by ¹H NMR analysis, using supramolecular complexation of pyrene-<i>d</i>₁₀ at the NDI residues to amplify the separation of resonances associated with different sequences. In such systems, pyrene is able to act as a "reader-molecule" by generating different levels of ring-current shielding from the different patterns of supramolecular binding to all the NDI-centred sequences of a given length.

Sequence-Modification in Copoly(ester-Imide)s: A Catalytic/supramolecular Approach to Writing/reading Copolymer Sequence-Information

Catalytic ester-interchange reactions, analogous to mutation and recombination, allow new sequence-information to be written, statistically, into NDI-based poly(ester-imide) chains. Thus, insertion of the cyclic ester cyclopentadecanolide ("exaltolide") into an NDI-based homopolymer, and quantitative sequence-exchange between two different homopoly(ester-imide)s, are catalysed by di-<i>n</i>-butyl tin(IV) oxide. Emerging sequences are identified at the triplet and quintet levels by ¹H NMR analysis, using supramolecular complexation of pyrene-<i>d</i>₁₀ at the NDI residues to amplify the separation of resonances associated with different sequences. In such systems, pyrene is able to act as a "reader-molecule" by generating different levels of ring-current shielding from the different patterns of supramolecular binding to all the NDI-centred sequences of a given length.

Process systems for the carbonate interchange reactions of DMC and alcohols: efficient synthesis of catechol carbonate

Reactive methanol removal either by adsorption or by azeotropic distillation promotes complete conversion of different alcohols to the corresponding carbonates.

The design of efficient carbonate interchange reactions with catechol carbonate

Catechol carbonate (CC) has been investigated as an innovative and highly active reactant for carbonate interchange reactions (CIRs).

Photo-responsive liquid crystalline epoxy networks with exchangeable disulfide bonds

Disulfide exchange and thiol–disulfide interchange reactions allow for reprocessing and recycling of azobenzene-based liquid crystalline networks.

Mechanisms of the S/CO/Se interchange reactions at FeMo-co, the active site cluster of nitrogenase

Mechanisms are developed for the observations of extraordinary substitution of bridging S by CO and Se, and the migration of Se, in the CFe7MoS9cluster at the active site of nitrogenase.