The role of hydrophobicity in supramolecular polymer/surfactant catalysts: An understandable model for enzymatic catalysis.

Autor: Costa PFA; Department of Chemistry, Universidade Federal de Santa Catarina, Florianópolis 88040-900, SC, Brazil., de Abreu R; Department of Chemistry, Universidade Federal de Santa Catarina, Florianópolis 88040-900, SC, Brazil., Fontana AB; Department of Chemistry, Universidade Federal de Santa Catarina, Florianópolis 88040-900, SC, Brazil., Fiedler HD; Department of Chemistry, Universidade Federal de Santa Catarina, Florianópolis 88040-900, SC, Brazil., Kirby AJ; Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK., Quina FH; Institute of Chemistry, University of São Paulo, CEP 05508-000 São Paulo, Brazil., Nome F; Department of Chemistry, Universidade Federal de Santa Catarina, Florianópolis 88040-900, SC, Brazil., Gerola AP; Department of Chemistry, Universidade Federal de Santa Catarina, Florianópolis 88040-900, SC, Brazil. Electronic address: adriana.gerola@ufsc.br.
Jazyk: angličtina
Zdroj: Journal of colloid and interface science [J Colloid Interface Sci] 2021 Apr 15; Vol. 588, pp. 456-468. Date of Electronic Publication: 2020 Dec 29.
DOI: 10.1016/j.jcis.2020.12.081
Abstrakt: Enzymes are highly significant catalysts, essential to biological systems, and a source of inspiration for the design of artificial enzymes. Although many models have been developed describing enzymatic catalysis, a deeper understanding of these biocatalysts remains a major challenge. Herein we detail the formation, characterization, performance, and catalytic mechanisms of a series of bio-inspired supramolecular polymer/surfactant complexes acting as artificial enzymes. The supramolecular complexes were characterized and exhibited exceptional catalytic efficiency for the dephosphorylation of an activated phosphate diester, the reaction rate being highly responsive to: (a) pH, (b) surfactant concentration, and (c) the length of the hydrophobic chain of the surfactant. Under optimal conditions (at pH > 8 for the more hydrophobic systems and at pre-micellar concentrations), enzyme-like rate enhancements of up to 6.0 × 10 9 -fold over the rate of the spontaneous hydrolysis reaction in water were verified. The catalytic performance is a consequence of synergy between the hydrophobicity of the aggregates and the catalytic functionalities of the polymer and the catalytic mechanism is modulated by the nature of the hydrophobic pockets of these catalysts, changing from a general base mechanism to a nucleophilic mechanism as the hydrophobicity increases. Taken as a whole, the present results provide fundamental insights, through an understandable model, which are highly relevant to the design of novel bioinspired enzyme surrogates with multifunctional potentialities for future practical applications.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2020 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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