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Biomimetic selenocystine based dynamic combinatorial chemistry for thiol-disulfide exchange.

ABSTRACT: Dynamic combinatorial chemistry applied to biological environments requires the exchange chemistry of choice to take place under physiological conditions. Thiol-disulfide exchange, one of the most popular dynamic combinatorial chemistries, usually needs long equilibration times to reach the required equilibrium composition. Here we report selenocystine as a catalyst mimicking Nature's strategy to accelerate thiol-disulfide exchange at physiological pH and low temperatures. Selenocystine is able to accelerate slow thiol-disulfide systems and to promote the correct folding of an scrambled RNase A enzyme, thus broadening the practical range of pH conditions for oxidative folding. Additionally, dynamic combinatorial chemistry target-driven self-assembly processes are tested using spermine, spermidine and NADPH (casting) and glucose oxidase (molding). A non-competitive inhibitor is identified in the glucose oxidase directed dynamic combinatorial library.

SUBMITTER: Canal-Martin A

PROVIDER: S-EPMC7794297 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

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Biomimetic selenocystine based dynamic combinatorial chemistry for thiol-disulfide exchange.

Canal-Martín Andrea A Pérez-Fernández Ruth R

Nature communications 20210108 1

Dynamic combinatorial chemistry applied to biological environments requires the exchange chemistry of choice to take place under physiological conditions. Thiol-disulfide exchange, one of the most popular dynamic combinatorial chemistries, usually needs long equilibration times to reach the required equilibrium composition. Here we report selenocystine as a catalyst mimicking Nature's strategy to accelerate thiol-disulfide exchange at physiological pH and low temperatures. Selenocystine is able ...[more]

PMID: 33420034

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