6 research outputs found
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Cucurbit[7]uril as a Supramolecular Artificial Enzyme for Diels–Alder Reactions
The ability to mimic the activity of natural enzymes using supramolecular constructs (artificial enzymes) is a vibrant scientific research field. Herein, we demonstrate that cucurbit[7]uril (CB[7]) can catalyse Diels–Alder reactions for a number of substituted and unreactive N-allyl-2-furfurylamines under biomimetic conditions, without the need for protecting groups, yielding powerful synthons in previously unreported mild conditions. CB[7] rearranges the substrate in a highly reactive conformation and shields it from the aqueous environment, thereby mimicking the mode of action of a natural Diels–Alderase. These findings can be directly applied to the phenomenon of product inhibition observed in natural Diels–Alderase enzymes, and pave the way toward the development of novel, supramolecular-based green catalysts.O.A.S. and A.P. acknowledge an ERC starting investigator grant (ASPiRe 240629) and EPSRC Programme Grant (NOtCH, EP/L027151/1) for the support, G.W. thanks the Leverhulme Trust (Natural material innovation for sustainable living) for the support, S.J.B. thanks the European Commission for a Marie Curie Fellowship (NANOSPHERE, 658360), E.R. gratefully acknowledges financial support from EPSRC (EP/N020669/1), E.M. and X.L. acknowledge the American Chemical Society Petroleum Research Fund (PRF No. 51053-ND4), the Department of Chemistry and Biochemistry, the College of Arts and Sciences and the Vice President for Research at Ohio University
Recommended from our members
Cucurbit[7]uril as a Supramolecular Artificial Enzyme for Diels–Alder Reactions
The ability to mimic the activity of natural enzymes using supramolecular constructs (artificial enzymes) is a vibrant scientific research field. Herein, we demonstrate that cucurbit[7]uril (CB[7]) can catalyse Diels–Alder reactions for a number of substituted and unreactive N-allyl-2-furfurylamines under biomimetic conditions, without the need for protecting groups, yielding powerful synthons in previously unreported mild conditions. CB[7] rearranges the substrate in a highly reactive conformation and shields it from the aqueous environment, thereby mimicking the mode of action of a natural Diels–Alderase. These findings can be directly applied to the phenomenon of product inhibition observed in natural Diels–Alderase enzymes, and pave the way toward the development of novel, supramolecular-based green catalysts.O.A.S. and A.P. acknowledge an ERC starting investigator grant (ASPiRe 240629) and EPSRC Programme Grant (NOtCH, EP/L027151/1) for the support, G.W. thanks the Leverhulme Trust (Natural material innovation for sustainable living) for the support, S.J.B. thanks the European Commission for a Marie Curie Fellowship (NANOSPHERE, 658360), E.R. gratefully acknowledges financial support from EPSRC (EP/N020669/1), E.M. and X.L. acknowledge the American Chemical Society Petroleum Research Fund (PRF No. 51053-ND4), the Department of Chemistry and Biochemistry, the College of Arts and Sciences and the Vice President for Research at Ohio University
Reversible biofunctionalization of surfaces with a switchable mutant of avidin
Label-free biosensors detect binding of prey molecules (″analytes″) to immobile bait molecules on the sensing surface. Numerous methods are available for immobilization of bait molecules. A convenient option is binding of biotinylated bait molecules to streptavidin-functionalized surfaces, or to biotinylated surfaces via biotin-avidin-biotin bridges. The goal of this study was to find a rapid method for reversible immobilization of biotinylated bait molecules on biotinylated sensor chips. The task was to establish a biotin-avidin-biotin bridge which was easily cleaved when desired, yet perfectly stable under a wide range of measurement conditions. The problem was solved with the avidin mutant M96H which contains extra histidine residues at the subunit-subunit interfaces. This mutant was bound to a mixed self-assembled monolayer (SAM) containing biotin residues on 20% of the oligo(ethylene glycol)-terminated SAM components. Various biotinylated bait molecules were bound on top of the immobilized avidin mutant. The biotin-avidin-biotin bridge was stable at pH ≥3, and it was insensitive to sodium dodecyl sulfate (SDS) at neutral pH. Only the combination of citric acid (2.5%, pH 2) and SDS (0.25%) caused instantaneous cleavage of the biotin-avidin-biotin bridge. As a consequence, the biotinylated bait molecules could be immobilized and removed as often as desired, the only limit being the time span for reproducible chip function when kept in buffer (2-3 weeks at 25 °C). As expected, the high isolectric pH (pI) of the avidin mutant caused nonspecific adsorption of proteins. This problem was solved by acetylation of avidin (to pI > 5), or by optimization of SAM formation and passivation with biotin-BSA and BSA