Rate enhancement of the oxidative folding of lysozyme by the use of aromatic thiol containing redox buffers

Gurbhele-Tupkar, Minakshi C.; Perez, Lissette R.; Silva, Yenia; Lees, Watson J.

doi:10.1016/j.bmc.2007.11.047

Cited by 24 publications

(24 citation statements)

References 56 publications

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“…Recently, improved redox buffers have been used, such as aliphatic dithiols, synthetic peptides, and aromatic monothiols. 32,[34][35][36][37][38]116 Aliphatic dithiols, e.g. Furthermore, in previous studies by our group, it has been shown that aromatic monothiols (pK a 5.5-6.6) increased the folding rate and the overall yield of native protein compared to standard aliphatic thiols (pK a 8.5-10).…”

Section: Redox Buffermentioning

confidence: 85%

“…Mono QAS 3 increased the folding rate and yield of reduced lysozyme (0.1 mg/mL as well at 1 mg/mL). 37,38 Hence, new aromatic dithiols (16 and 17) similar in structure to the Mono QAS 3 were designed, having one thiol group on each of the two aromatic rings and the two aromatic rings connected by a hydrocarbon chain containing two quaternary ammonium groups.…”

Section: Quaternary Ammonium Aromatic Dithiols (16 and 17)mentioning

confidence: 99%

“…Lysozyme was selected as this enzyme has been extensively studied, and its folding pathway has been well characterized. 37,85,129,[137][138][139] The folding of reduced lysozyme was carried out in the presence of various concentrations of aromatic dithiols (11, 12, 14, and 15) in combination with either 0.2 mM GSSG or 2 mM GSSG. These concentrations of GSSG were selected as our previous results obtained with RNase A and lysozyme used 0.2 mM or 2 mM GSSG.…”

mentioning

confidence: 99%

“…These concentrations of GSSG were selected as our previous results obtained with RNase A and lysozyme used 0.2 mM or 2 mM GSSG. 4,[35][36][37] These folding experiments were then compared directly with 7 mM GSH and 2 mM GSSG. These concentrations of GSH and GSSG were selected for the folding experiments as they gave the best combination of folding rate and yield in our previous study at 0.1 mg/mL lysozyme concntration.…”

mentioning

confidence: 99%

“…These concentrations of GSH and GSSG were selected for the folding experiments as they gave the best combination of folding rate and yield in our previous study at 0.1 mg/mL lysozyme concntration. 37 All the folding experiments were carried out at pH 7.0 and 8.0, and 0.1 mg/mL (7 µM) lysozyme concentration at 25 o C.…”

mentioning

confidence: 99%

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Synthesis of Aromatic Monothiols and Aromatic Dithiols to Increase the Folding Rate and Yield of Disulfide Containing Proteins

Patel¹

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Section: Redox Buffermentioning

confidence: 85%

Section: Quaternary Ammonium Aromatic Dithiols (16 and 17)mentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Synthesis of Aromatic Monothiols and Aromatic Dithiols to Increase the Folding Rate and Yield of Disulfide Containing Proteins

Patel¹

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An Amphiphilic Selenide Catalyst Behaves Like a Hybrid Mimic of Protein Disulfide Isomerase and Glutathione Peroxidase 7

Arai

Moriai

Ogawa

et al. 2014

Chemistry An Asian Journal

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Protein disulfide isomerase (PDI) and glutathione peroxidase 7 (GPx7) cooperatively promote the oxidative folding of disulfide (SS)-containing proteins in endoplasmic reticulum by recognizing the nascent proteins to convert them into the native folds by means of SS formation and SS isomerization and by catalyzing reoxidation of reduced PDI with H2O2, respectively. In this study, new amphiphilic selenides with a long-chain alkyl group were designed as hybrid mimics of PDI and GPx7 and were applied to the refolding of reduced hen egg-white lysozyme (HEL-R). Competitive SS formation at pH 4 using HEL-R and glutathione (GSH) in the presence of the selenide catalyst and H2O2 showed that the amphiphilic selenides can preferentially catalyze SS formation of HEL-R, probably on account of hydrophobic interactions between the protein and the catalyst. In contrast, simple water-soluble selenides did not exhibit such behavior. In addition, when the pH of the solution was adjusted to 8.5 after the SS formation, surviving GSH promoted the SS isomerization of misfolded HEL to recover the native SS linkages. Thus, the amphiphilic selenides designed here could mimic the function of the PDI-GPx7 system. The combination of a water-soluble selenide and a long-chain alkyl group would be a useful motif in designing medicines for both protein misfolding diseases and antioxidant therapy.

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Basic Amino Acid Conjugates of 1,2‐Diselenan‐4‐amine with Protein Disulfide Isomerase‐like Functions as a Manipulator of Protein Quality Control

Tsukagoshi

Mikami

Arai

2020

Chemistry An Asian Journal

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Protein disulfide isomerase (PDI) can assist immature proteins to correctly fold by controlling cysteinyl disulfide (SS)‐relating reactions (i. e., SS‐formation, SS‐cleavage, and SS‐isomerization). PDI controls protein quality by suppressing protein aggregation, as well as functions as an oxidative folding catalyst. Following the amino acid sequence of the active center in PDI, basic amino acid conjugates of 1,2‐diselenan‐4‐amine (1), which show oxidoreductase‐ and isomerase‐like activities for SS‐relating reactions, were designed as a novel PDI model compound. By conjugating the amino acids, the diselenide reduction potential of compound 1 was significantly increased, causing improvement of the catalytic activities for all SS‐relating reactions. Furthermore, these compounds, especially histidine‐conjugated one, remarkably suppressed protein aggregation even at low concertation (0.3 mM∼). Thus, it was demonstrated that the conjugation of basic amino acids into 1 simultaneously achieves the enhancement of the redox reactivity and the capability to suppress protein aggregation.

show abstract

Rate enhancement of the oxidative folding of lysozyme by the use of aromatic thiol containing redox buffers

Cited by 24 publications

References 56 publications

Synthesis of Aromatic Monothiols and Aromatic Dithiols to Increase the Folding Rate and Yield of Disulfide Containing Proteins

Synthesis of Aromatic Monothiols and Aromatic Dithiols to Increase the Folding Rate and Yield of Disulfide Containing Proteins

An Amphiphilic Selenide Catalyst Behaves Like a Hybrid Mimic of Protein Disulfide Isomerase and Glutathione Peroxidase 7

Basic Amino Acid Conjugates of 1,2‐Diselenan‐4‐amine with Protein Disulfide Isomerase‐like Functions as a Manipulator of Protein Quality Control

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