Abstract
In peptide production, oxidative sulfitolysis can be used to protect the cysteine residues during purification, and the introduction of a negative charge aids solubility. Subsequent controlled reduction aids in ensuring correct disulfide bridging. In vivo, these problems are overcome through interaction with chaperones. Here, a versatile peptide production process has been developed using an angled vortex fluidic device (VFD), which expands the viable pH range of oxidative sulfitolysis from pH 10.5 under batch conditions, to full conversion within 20 min at pH 9–10.5 utilising the VFD. VFD processing gave 10-fold greater conversion than using traditional batch processing, which has potential in many applications of the sulfitolysis reaction.
Highlights
Oxidative sulfitolysis introduces negatively charged sulfonate moieties onto a peptide chain containing cysteine residues [1,2]
Oxidative sulfitolysis was performed on oxytocin using the following procedure
IGF, insulin-like growth factor; RT, room temperature; O/N, overnight. This widely used reaction in protein production and purification gave >10-fold conversion using vortex fluidic device (VFD) processing than previously reported using traditional batch methods. This is significant given that the extent of recovery of biological activity is important in many applications of the sulfitolysis reaction
Summary
Oxidative sulfitolysis introduces negatively charged sulfonate moieties onto a peptide chain containing cysteine residues [1,2]. This increases the solubility and stability of proteins, and is especially useful for processing proteins with multiple cysteine residues [3,4,5]. The oxidative sulfitolysis of cysteine residues in proteins involves treatment with sodium sulphite and an oxidizing agent, typically sodium tetrathionate or potassium o-iodobenzoate. The use of a sulfitolysis step can enhance the efficiency of this processing to achieve the properly folded protein with the desired activity, efficacy, and affinity levels [13]
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