Application of ATR-FTIR as a screening method for analysis of biopharmaceutical preparations containing trastuzumab

Hrisanta Godzo, Olga Gigopulu, Jelena Acevska, Nikola Geskovski, Ana Poceva Panovska, Bobi Acevski, Frosina Dimoska, Marija Nuneva, Katerina Brezovska
{"title":"Application of ATR-FTIR as a screening method for analysis of biopharmaceutical preparations containing trastuzumab","authors":"Hrisanta Godzo, Olga Gigopulu, Jelena Acevska, Nikola Geskovski, Ana Poceva Panovska, Bobi Acevski, Frosina Dimoska, Marija Nuneva, Katerina Brezovska","doi":"10.33320/maced.pharm.bull.2023.69.03.124","DOIUrl":null,"url":null,"abstract":"In recent years, the number of therapeutic proteins introduced to the biopharmaceutical market has increased significantly, as medicine research and development have focused on protein-based therapies. Along with the introduction of biosimilar and biobetter medicines, the competitiveness of the biopharmaceutical market has grown considerably (Torres-Obreque et al., 2022). As a result, there is a global emergence of falsified biopharmaceuticals, especially monoclonal antibodies (mAbs), including trastuzumab, a humanized IgG1 mAb used as HER2-targeted therapy for the treatment of breast cancer (Maadi et al., 2021). In most of the seized falsified samples of medicines declared to contain mAbs (trastuzumab, rituximab, bevacizumab), no active pharmaceutical ingredient (API) was detected (Janvier et al, 2018). Therefore, suitable testing strategy and workflow should be defined in cases where falsification is suspected. Taking into account that mAbs are predominantly glycoproteins of high molecular weight (~ 150 kDa) with complex higher-order structure, their characterization can be rather challenging. Most of the analytical methods used for protein identification and characterization of mAbs (chromatography, electrophoresis, mass spectrometry and nuclear magnetic resonance) are time-consuming, expensive and require extensive sample preparation (Alhazmi et al., 2023). Therefore, implementation of fast, simple, and direct screening tools is of vast importance for the analytical quality control of these medicines. The use of vibrational spectroscopic techniques, particularly infrared (Hamla et al., 2022) for characterization of mAbs is drawing more attention since these are rapid and non-destructive methods. In this study, we demonstrate the potential use of Fourier transform infrared (FTIR) spectrophotometry, with attenuated total reflectance (ATR) for identification of trastuzumab in biopharmaceutical preparations.","PeriodicalId":30550,"journal":{"name":"Makedonsko Farmacevtski Bilten","volume":"77 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2023-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Makedonsko Farmacevtski Bilten","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.33320/maced.pharm.bull.2023.69.03.124","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

In recent years, the number of therapeutic proteins introduced to the biopharmaceutical market has increased significantly, as medicine research and development have focused on protein-based therapies. Along with the introduction of biosimilar and biobetter medicines, the competitiveness of the biopharmaceutical market has grown considerably (Torres-Obreque et al., 2022). As a result, there is a global emergence of falsified biopharmaceuticals, especially monoclonal antibodies (mAbs), including trastuzumab, a humanized IgG1 mAb used as HER2-targeted therapy for the treatment of breast cancer (Maadi et al., 2021). In most of the seized falsified samples of medicines declared to contain mAbs (trastuzumab, rituximab, bevacizumab), no active pharmaceutical ingredient (API) was detected (Janvier et al, 2018). Therefore, suitable testing strategy and workflow should be defined in cases where falsification is suspected. Taking into account that mAbs are predominantly glycoproteins of high molecular weight (~ 150 kDa) with complex higher-order structure, their characterization can be rather challenging. Most of the analytical methods used for protein identification and characterization of mAbs (chromatography, electrophoresis, mass spectrometry and nuclear magnetic resonance) are time-consuming, expensive and require extensive sample preparation (Alhazmi et al., 2023). Therefore, implementation of fast, simple, and direct screening tools is of vast importance for the analytical quality control of these medicines. The use of vibrational spectroscopic techniques, particularly infrared (Hamla et al., 2022) for characterization of mAbs is drawing more attention since these are rapid and non-destructive methods. In this study, we demonstrate the potential use of Fourier transform infrared (FTIR) spectrophotometry, with attenuated total reflectance (ATR) for identification of trastuzumab in biopharmaceutical preparations.
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
应用ATR-FTIR筛选方法分析含曲妥珠单抗的生物药物制剂
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
25
审稿时长
10 weeks
期刊最新文献
Step by Step Preparation and Optimization of Lysozyme Hydrophobic Ion Pairing Complex Principal Component Analysis to evaluate the stability impact of protein mutations: the case of SARS-CoV-2 K417T mutation The Impact of the Human Microbiome on Cancer Immunotherapy Design and optimization of a chitosan coated nanostructured lipid carriers of paliperidone Synthesis and evaluation of lipid peroxidase inhibition of 4-methyl substituted coumarins
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1