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Dissecting the stability of Atezolizumab with renewable amino acid-based ionic liquids: Colloidal stability and anticancer activity under thermal stress

化学 离子液体 热稳定性 生物制药 动态光散射 氨基酸 核化学 色谱法 化学工程 有机化学 纳米颗粒 生物化学 催化作用 工程类 生物 遗传学
作者
Bayan Alkhawaja,Faisal Al‐Akayleh,Zaid Al-Rubaye,Ghayda' AlDabet,Muna Bustami,Maisa’a Smairat,Ahmed S.A. Ali Agha,Jehad Nasereddin,Nidal A. Qinna,A Mikhaluta Michael,Andrew G. Watts
出处
期刊:International Journal of Biological Macromolecules [Elsevier]
卷期号:270: 132208-132208 被引量:5
标识
DOI:10.1016/j.ijbiomac.2024.132208
摘要

Monoclonal antibodies (mAbs) have revolutionised the biopharmaceutical market. Being proteinaceous, mAbs are prone to chemical and physical instabilities. Various approaches were attempted to stabilise proteins against degradation factors. Ionic liquids (ILs) and deep eutectic solvents (DESs) have been established as green solvents for ever-increasing pharmaceutical and biopharmaceutical applications. Hence, amino acid (AA)-based ILs, were used for the first time, for mAb stabilisation. Choline (Ch)-based DESs were also utilised for comparison purposes. The prepared ILs and DESs were utilised to stabilise Atezolizumab (Amab, anti-PDL-1 mAb). The formulations of Amab in ILs and DESs were incubated at room temperature, 45 or 55 °C. Following this, the structural stability of Amab was appraised. Interestingly, Ch-Valine retained favourable structural stability of Amab with minimal detected aggregation or degradation as confirmed by UV-visible spectroscopy and protein Mass Spectroscopy. The measured hydrodynamic diameter of Amab in Ch-Valine ranged from 10.40 to 11.65 nm. More interestingly, the anticancer activity of Amab was evaluated, and Ch-Valine was found to be optimum in retaining the activity of Amab when compared to other formulations, including the control Amab sample. Collectively, this study has spotlighted the advantages of adopting the Ch-AA ILs for the structural and functional stabilising of mAbs.
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