强制氧化抗VEGF IgG分子的分析研究:聚焦于抗原和受体结合活性的改变

IF 2.3 Q3 PHARMACOLOGY & PHARMACY Scientia Pharmaceutica Pub Date : 2023-06-28 DOI:10.3390/scipharm91030031
A. Parlar, B. Gurel, Mehmet Reşit Sönmez, Meral Yüce
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引用次数: 0

摘要

分子在应激条件下的生物活性变化尚未在文献中得到广泛的记录。本研究旨在揭示各种氧化条件对商业抗VEGF IgG分子mAb模型的功能影响。研究了对抗原结合、细胞增殖、FcRn受体和C1q结合的反应,这些反应在当前文献中很少出现。作者报告了mAb在各种应激条件下的肽图谱数据、翻译后修饰(PTM)分析、细胞增殖性能以及抗原(VEGF)、C1q和FcRn结合活性。mAb的易氧化位点被确定为DTLMISR肽中的Met252。mAb的VEGF结合活性和抗细胞增殖活性没有改变,而C1q和FcRn结合能力在氧化应激条件下显著降低。完整的报告对于mAb的许多科学和工业过程至关重要。作者建议在研究应激因素对治疗性单克隆抗体的影响时,除了进行结构研究外,还进行功能分析。
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Analytical Investigation of Forced Oxidized Anti-VEGF IgG Molecules: A Focus on the Alterations in Antigen and Receptor Binding Activities
Alterations in the biological activity of the molecules under stress conditions have not been documented as widely in the literature yet. This study was designed to reveal the functional impacts of various oxidation conditions on a model mAb, a commercial anti-VEGF IgG molecule. The responses to antigen binding, cell proliferation, FcRn receptors, and C1q binding, which rarely appear in the current literature, were investigated. The authors report peptide mapping data, post-translational modification (PTM) analysis, cell proliferation performance, and antigen (VEGF), C1q, and FcRn binding activities of the mAb under various stress conditions. The oxidation-prone site of the mAb was determined as Met252 in the DTLMISR peptide. The VEGF binding activity and anti-cell proliferation activity of the mAbs did not alter, while C1q and FcRn binding capacity significantly decreased under oxidative stress conditions. The full report is vital for many scientific and industrial processes about mAbs. The authors recommend performing functional analyses in addition to the structural studies while investigating the impacts of stress factors on therapeutic mAbs.
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来源期刊
Scientia Pharmaceutica
Scientia Pharmaceutica Pharmacology, Toxicology and Pharmaceutics-Pharmaceutical Science
CiteScore
4.60
自引率
4.00%
发文量
67
审稿时长
10 weeks
期刊最新文献
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