Collectively, the recombinant PDI protein exhibits good biocompatibility and pro-adhesive activity, demonstrating its potential as a candidate raw material for skin-repair cosmetics.
Abstract
To investigate the potential of recombinant protein disulfide isomerase (PDI) as a raw material for skin-repair cosmetics, an engineered PDI-producing strain was constructed using the Pichia pastoris X33 expression system. The target protein was obtained through methanol-induced expression and anion-exchange chromatography purification, and its cytotoxicity and pro-adhesive effects on human skin fibroblasts (HSFs) were evaluated. The results showed that the purified recombinant PDI protein had an apparent molecular weight of approximately 55.7 kDa. Treatment with 0.04–5 µmol/L recombinant PDI for 24 h did not affect cell viability. On culture surfaces coated with 62.5 nmol/L recombinant human fibronectin (rhFN) or 31.25 nmol/L recombinant human collagen (rhC), the addition of 250 nmol/L recombinant PDI increased the HSF adhesion area ratio to approximately 2.1-fold that of the rhFN-alone group (p < 0.0001) and 1.9-fold that of the rhC-alone group (p < 0.0001). Collectively, the recombinant PDI protein exhibits good biocompatibility and pro-adhesive activity, demonstrating its potential as a candidate raw material for skin-repair cosmetics.
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A new machine-learning framework aims to improve the success rate of computational protein design while moving away from results that reproduce sequences found in nature.