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Alternating Current Electrolysis for the Electrocatalytic Synthesis of Mixed Disulfide via Sulfur-Sulfur Bond Metathesis towards Dynamic Disulfide Libraries.

ABSTRACT: A novel approach of electrolysis using alternating current was applied in the sulfur-sulfur bond metathesis of symmetrical disulfides towards unsymmetrical disulfides. As initially expected, a statistical distribution in disulfides was obtained. Furthermore, the influence of electrode polarisation by alternating current was investigated on a two-disulfide matrix. The highly dynamic nature of this chemistry resulted in the creation of dynamic disulfide libraries by expansion of the matrices, consisting of up to six symmetrical disulfides. In addition, mixing of matrices and stepwise expanding of a matrix by using alternating current electrolysis were realised.

SUBMITTER: Sattler LE

PROVIDER: S-EPMC7079035 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Alternating Current Electrolysis for the Electrocatalytic Synthesis of Mixed Disulfide via Sulfur-Sulfur Bond Metathesis towards Dynamic Disulfide Libraries.

Sattler Lars Erik LE Otten Chris Josef CJ Hilt Gerhard G

Chemistry (Weinheim an der Bergstrasse, Germany) 20200218 14

A novel approach of electrolysis using alternating current was applied in the sulfur-sulfur bond metathesis of symmetrical disulfides towards unsymmetrical disulfides. As initially expected, a statistical distribution in disulfides was obtained. Furthermore, the influence of electrode polarisation by alternating current was investigated on a two-disulfide matrix. The highly dynamic nature of this chemistry resulted in the creation of dynamic disulfide libraries by expansion of the matrices, cons ...[more]

PMID: 31908043

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Project description:The protein secretory pathway must maintain homoeostasis while producing a wide assortment of proteins in different conditions. It is also used extensively to produce many useful proteins in biotechnology. As such, secretory pathway dysfunction can be highly detrimental to the cell, resulting in the molecular basis for many human diseases, and can drastically inhibit product titers in biochemical production. Because the secretory pathway is a highly-integrated, multi-organelle system, dysfunction can happen at many levels and dissecting the root cause can be challenging. To better understand some of these dysfunctions, we measured multiple systems-level states of the cell (physiology, transcriptome, metabolism) while secreting a small protein (insulin precursor) or a large protein (?-amylase). This was carried out in the presence and absence of HAC1, a key transcription factor in maintaining secretory homeostasis. Clear trends in cellular stress were apparent across multiple data resulting from our perturbations. In particular, processes involving (1) degradation of protein / recycling amino acids, (2) overall transcription/translation repression, and (3) oxidative stress. Apparent runaway oxidative radical production was explained by a thermodynamic model that we put forward for disulfide formation in the endoplasmic reticulum. This model predicts that balancing the relative rates of protein folding and disulfide bond formation are key to easing oxidative stress. These predictions have direct implications in how to engineer a broad range of recombinant proteins for secretion and provide potential hypotheses for the root causes of several secretory-associated diseases. Yeast strains were constructed that produce and secrete (a) IP or (b) ?-amylase and were compared to yeast strains containing (c) an empty vector in both wild-type and HAC1 deletion backgrounds. These strains are named WN (WT with empty vector), WI (WT secreting IP), WA (WT secreting ?-amylase), dN (?hac1 with empty vector), dI (?hac1 secreting IP), and dA (?hac1 secreting ?-amylase). Strains were characterized in batch fermentation and samples were taken in mid-exponential phase. Triplicate fermentations were carried out for each strain.

Dataset Information

Alternating Current Electrolysis for the Electrocatalytic Synthesis of Mixed Disulfide via Sulfur-Sulfur Bond Metathesis towards Dynamic Disulfide Libraries.

Publications

Alternating Current Electrolysis for the Electrocatalytic Synthesis of Mixed Disulfide via Sulfur-Sulfur Bond Metathesis towards Dynamic Disulfide Libraries.

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