Evidence map›Paper›PMID 40080266›Full record

ArticleMolecular biology reports2025

Site-specific PEGylation of recombinant protein SAC-TRAIL and characterization of the effect on antitumor activity.

Shuting Pan, Yuguo Dong, Xuedong Wang, Yuhong Ren, Zebo Xiu, Jian Zhang

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Article in Molecular biology reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Shuting PanState Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
Yuguo DongState Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
Xuedong WangState Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
Yuhong RenState Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China.
Zebo XiuLiaocheng People's Hospital, Liaocheng, Shandong, 252000, China. 976230141@qq.com.
Jian ZhangState Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, China. zhangjian0020@ecust.edu.cn.

Funding

National Natural Science Foundation of China No. 21706072Natural Science Foundation of Shanghai 22ZR1418300
6 · The paper itself

Abstract

backgroundTumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a promising anti-tumor agent with selective cytotoxicity across a broad spectrum of tumor cell lines. In previous studies, we engineered a recombinant protein drug, SAC-TRAIL, which significantly enhanced the antitumor activity of TRAIL without exhibiting toxicity to normal cells. However, its application in cancer therapy is restricted due to poor resistance to proteolytic degradation and a limited in vivo half-life. METHODS AND

resultsTo address these limitations, we designed a site-specific PEGylation method by conjugating methoxy-polyethylene glycol maleimide (mPEG-MAL) to the thiol group of specific cysteine residues on SAC-TRAIL. In this study, we optimized the PEGylation conditions for SAC-TRAIL, evaluated the in vitro activity and stability of mPEG-MAL-SAC-TRAIL, and conducted in vivo studies to assess its antitumor efficacy. It was shown that approximately 95% of SAC-TRAIL was PEGylated by mPEG-MAL within 30 min, exhibiting improved in vitro stability and antitumor activity. Furthermore, mPEG-MAL-SAC-TRAIL demonstrated enhanced anti-tumor activity and stability in an animal tumor model.

conclusionsIn summary, site-specific PEGylation at Cys-SH residues offers a promising strategy for extending the effective duration of SAC-TRAIL.

Indexed as

Antineoplastic AgentsPolyethylene GlycolsTNF-Related Apoptosis-Inducing LigandAnimalsApoptosisCell Line, TumorFemaleHumansMaleimidesMiceMice, Inbred BALB CMice, NudeRecombinant Fusion ProteinsRecombinant ProteinsXenograft Model Antitumor AssaysAntineoplastic AgentsmaleimideMaleimidesPolyethylene GlycolsRecombinant Fusion ProteinsRecombinant ProteinsTNF-Related Apoptosis-Inducing LigandCancer therapymPEG-MALRecombinant proteinSite-specific modificationStability

Identifiers

PMID40080266

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