{
  "abstract": "Production of commercial antibodies commonly relies on mammalian expression platforms; however, these are associated with high production costs and technical challenges during large-scale cultivation. In this study, we aimed to develop an Escherichia coli-based platform for the production of an anti-PD-L1 single-chain variable fragment, hereafter aPD-L1 scFv. Expression of aPD-L1 scFv in E. coli BL21(DE3) resulted in extensive inclusion body formation regardless of the expression temperatures at 16 °C, 30 °C, and 37 °C, with approximately 84-93% accumulating in the insoluble fraction. To improve its solubility, co-expression with several molecular chaperones, namely DnaK-DnaJ-GrpE and GroES-GroEL, was investigated. Optimization of L-arabinose concentrations as an inducer for DnaK-DnaJ-GrpE expression demonstrated that induction at 0.15 mg/mL increased aPD-L1 scFv solubility from 5.13% to 23.97%, although the difference was not statistically significant. Moreover, His-tag purification yielded 14.78 µg/mL and 18.62 µg/mL without and with molecular chaperone co-expression, respectively. The binding activity of purified aPD-L1 scFv was confirmed by ELISA, which showed comparable binding signals following chaperone-assisted expression. This indicated that the functional activity was retained. Altogether, these findings suggest that molecular chaperone co-expression has the potential to increase the soluble production of functional aPD-L1 scFv in E. coli, supporting the feasibility of bacterial expression systems as a cost-effective platform for recombinant antibody fragment production.",
  "abstract_shown": true,
  "affiliations": [
    "Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand.",
    "Cell Engineering for Cancer Therapy Research Group, Chiang Mai University, Chiang Mai 50200, Thailand."
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Sarinthip Khamthiang"
    },
    {
      "affs": [
        0
      ],
      "name": "Chonlaphon Juntama"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Aussara Panya"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Pachara Sattayawat",
      "orcid": "0000-0003-1272-544X"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/b0zfgzbqqqx9m.bib",
  "cited_by": 0,
  "doi": "10.3390/life16101664",
  "fulltext_url": "https://europepmc.org/articles/PMC13705652",
  "id": "b0zfgzbqqqx9m",
  "issns": [
    "2075-1729"
  ],
  "landing_url": "https://europepmc.org/article/MED/42942250",
  "language": "eng",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1312|Protein purification and stability"
    ]
  ],
  "openalex": "W7220361861",
  "pdf_url": "https://europepmc.org/articles/PMC13705652?pdf=render",
  "pmcid": "PMC13705652",
  "pmid": "42942250",
  "published": "2026-10-03",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/b0zfgzbqqqx9m.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:22:24Z",
      "native_id": "MED:42942250",
      "source": "europepmc",
      "url": "https://europepmc.org/article/MED/42942250"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Protein purification and stability",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Co-Expression of Molecular Chaperones to Enhance Soluble aPD-L1 scFv Production in Escherichia coli BL21(DE3).",
  "title_text": "Co-Expression of Molecular Chaperones to Enhance Soluble aPD-L1 scFv Production in Escherichia coli BL21(DE3).",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:22:24Z",
  "url": "https://research.draconitic.com/paper/b0zfgzbqqqx9m",
  "venue": "Life (Basel, Switzerland)",
  "versions": []
}