Chemical synthesis of human selenoprotein F and elucidation of its thiol-disulfide oxidoreductase activity

Liao, Peisi; Liu, Hongmei; He, Chunmao

doi:10.1039/d2sc00492e

Cited by 8 publications

(6 citation statements)

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“…4C-d, the ligation went to completion within 2 h, and product 24 was co-eluted with hydrolysis and truncation (at Met13) by-products. Nevertheless, without any purification, dialysis, or ultracentrifugation treatment, a rapid dilution strategy where the ligation mixture was added directly to a redox buffer 11 b ,30 (final protein conc., ∼0.3 mg mL −1 ) was adopted, and the refolding was allowed for 24 h at 4 °C (Fig. 4C-e).…”

Section: Resultsmentioning

confidence: 99%

“…In an effort to improve the overall yield, we consulted our previous work to carry out the ligation and refolding without intermediate HPLC purification. 11 b ,30 For this purpose, the ligation mixture was exchanged into a buffer containing 6 M Gdn·HCl and 0.2 M Na 2 HPO 4 (pH 6.0) by ultracentrifugation (3 kDa cut-off) and was directly added dropwise into the refolding buffer (final conc. 0.25 mg mL −1 ).…”

Section: Resultsmentioning

confidence: 99%

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Azole reagents enabled ligation of peptide acyl pyrazoles for chemical protein synthesis

Liao,

2024

Chem. Sci.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Azole reagents enabled ligation of peptide acyl pyrazoles for chemical protein synthesis

Liao,

2024

Chem. Sci.

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“…Meanwhile, fragment 21 was generated from the recombinant Mb(1–69)-CPG-His 6 ( 21a ) via S-cyanylation and hydrazinolysis , (Figure S26) and fragment 23 through N-terminal His 6 -SUMO fusion protein expression and Ulp1 cleavage (Figure S27). − …”

Section: Resultsmentioning

confidence: 99%

Oxidation and Phenolysis of Peptide/Protein C-Terminal Hydrazides Afford Salicylaldehyde Ester Surrogates for Chemical Protein Synthesis

Lin

Wang

et al. 2023

J. Am. Chem. Soc.

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With the growing popularity of serine/threonine ligation (STL) and cysteine/penicillamine ligation (CPL) in chemical protein synthesis, facile and general approaches for the preparation of peptide salicylaldehyde (SAL) esters are urgently needed, especially those viable for obtaining expressed protein SAL esters. Herein, we report the access of SAL ester surrogates from peptide hydrazides (obtained either synthetically or recombinantly) via nitrite oxidation and phenolysis by 3-(1,3-dithian-2-yl)-4-hydroxybenzoic acid (SAL(−COOH)PDT). The resulting peptide SAL(−COOH)PDT esters can be activated to afford the reactive peptide SAL(−COOH) esters for subsequent STL/CPL. While being operationally simple for both synthetic peptides and expressed proteins, the current strategy facilitates convergent protein synthesis and combined application of STL with NCL. The generality of the strategy is showcased by the N-terminal ubiquitination of the growth arrest and DNA damage-inducible protein (Gadd45a), the efficient synthesis of ubiquitin-like protein 5 (UBL-5) via a combined N-to-C NCL-STL strategy, and the C-to-N semisynthesis of a myoglobin (Mb) variant.

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“…The thiol-disulfide oxidoreductase activity of SELENOF was further supported by its ability to catalyze the reduction and isomerization of disulfide bonds. Moreover, we found that the presence of Sec in the redox motif was the key for this activity [ 37 ].…”

Section: Discussionmentioning

confidence: 99%

Selenoprotein F Knockout Caused Glucose Metabolism Disorder in Young Mice by Disrupting Redox Homeostasis

Yun

Zhou

et al. 2022

Antioxidants

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Selenoprotein F (SELENOF) might play an important role in maintaining human health since an increasing number of studies have linked SELENOF deficiency to various pathologies such as cancer and neurodegeneration. We have previously reported on glucose metabolism disorders in SELENOF knockout mice, which imply a novel biological function of SELENOF in glucose metabolism. However, the underlying mechanism and whether the effect of SELENOF on glucose metabolism is age-dependent remain unknown. In the present study, we compare the metabolic phenotype in more detail as well as the oxidative stress parameters in SELENOF knockout mice (C57BL/6J background) and naïve C57BL/6J mice of different ages (12, 16 and 21 weeks old). The results showed that SELENOF knockout caused glucose metabolism disorders only in young mice, especially in 12-week-old mice, characterized by hyperglycemia, serum insulin reduction, impaired glucose tolerance, decreased insulin sensitivity, decreased glucose catabolism, increased gluconeogenesis and impaired insulin signaling pathway. These abnormalities gradually improved with age and disappeared in knockout mice at 21 weeks old. Furthermore, before 16 weeks old, SELENOF knockout mice showed increased lipid peroxidation and decreased glutathione/glutathione disulfide ratio and glutathione peroxidase activity in the serum and liver. Furthermore, the expression of glutathione peroxidase 1 significantly reduced in the liver and pancreas. Our findings suggest that SELENOF knockout might cause glucose metabolism disorders in young mice via the disruption of redox homeostasis.

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Chemical synthesis of human selenoprotein F and elucidation of its thiol-disulfide oxidoreductase activity

Abstract: Selenoprotein F (SelF) is an endoplasmic reticulum-residing eukaryotic protein that contains a selenocysteine (Sec) residue. It has been suggested to be involved in a number of physiological processes by acting...

Cited by 8 publications

References 54 publications

Azole reagents enabled ligation of peptide acyl pyrazoles for chemical protein synthesis

Azole reagents enabled ligation of peptide acyl pyrazoles for chemical protein synthesis

Oxidation and Phenolysis of Peptide/Protein C-Terminal Hydrazides Afford Salicylaldehyde Ester Surrogates for Chemical Protein Synthesis

Selenoprotein F Knockout Caused Glucose Metabolism Disorder in Young Mice by Disrupting Redox Homeostasis

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