Peptide disulfide RKCGCFF facilitates oxidative protein refolding by mimicking protein disulfide isomerase |
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Institution: | 1. Instituto de Investigaciones en Catálisis y Petroquímica (INCAPE) (FIQ-UNL, CONICET), Colectora Ruta Nac. N° 168 km 0, Paraje El Pozo, CP 3000 Santa Fe, Argentina;2. Institut de Chimie des Milieux et des Matériaux de Poitiers (IC2MP), Université de Poitiers, UMR 7285 CNRS, 4 rue Michel Brunet, 86073 Poitiers Cedex 9, France |
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Abstract: | This communication reports a new design of peptide disulfide, RKCGCFF, for facilitating oxidative protein refolding. The new design mimics the properties of protein disulfide isomerase (PDI) by introducing hydrophobic and positively charged patches into the two terminals of disulfide CGC. RKCGCFF was found more effective than the traditional oxidant oxidized glutathione (GSSG) as well as its counterpart, RKCGC, in facilitating the oxidative refolding of lysozyme. More importantly, RKCGCFF could improve lysozyme refolding yield at a high concentration (0.7 mg/mL). The research proved that incorporation of hydrophobic and charged patches into the CGC disulfide made the oxidant more similar to PDI in structure and properties. |
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Keywords: | Protein Refolding Bioseparations Protein recovery Peptide disulfide Foldase mimic |
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