Biomimetic peptide functionalized affinity materials for mAbs capture and analysis

Zhengjin JIANG, Institute of Pharmaceutical Analysis, College of Pharmacy, JINAN UNIVERSITY, Guangzhou, china (jzjjackson@hotmail.com)
Qiqin WANG, Institute Of Pharmaceutical Analysis, College Of Pharmacy, Jinan University, Guangzhou, China
Xiao LIU, Institute Of Pharmaceutical Analysis, College Of Pharmacy, Jinan University, Guangzhou, China
Hao HUANG, Institute Of Pharmaceutical Analysis, College Of Pharmacy, Jinan University, Guangzhou, China

Therapeutic monoclonal antibodies (mAbs) are the fastest-growing category of new therapeutic drugs. In recent decades, antibody purification and capture were mainly performed using affinity chromatography. Protein A or G from bacterial sources are commonly used affinity ligands. However, there are still some drawbacks, such as high cost, leakage of ligands and not selective for specific mAbs^[1], to be overcome.  

In comparison with protein-based ligands, biomimetic peptides are particularly attractive because of their better chemical stability, lower cost and immunogenicity, rich functionality, wide structural diversity etc.. These peptides can be designed for specifically binding to Fc or Fab region of mAbs. In our recent studies, a series of biomimetic peptide ligands were successfully developed based on the complex of mAbs-antigen or mAbs-protein A. Biomimetic peptide ligands functionalized affinity materials were then fabricated through radical initiated co-polymerization. All affinity materials showed high affinity to their corresponding mAbs. For example, DAAG peptide functionalized monolith was successfully applied to specifically enrich and purify trastuzumab from CHO cell culture supernatant and IgG from human serum ^[2]. HH24 peptide binding to Fab region of trastuzumab could precisely distinguish between IgG and trastuzumab. The peptide (HH24) functionalized biomaterial could successfully capture trastuzumab in 3-folds diluted spiked human serum with high purity and recovery. Moreover, a simple detection method based on this novel biomaterial was also developed for the quantification of trastuzumab in the spiked human serum samples. In summary, biomimetic peptide functionalized affinity materials hold great promises for the purification and bioanalysis of target mAbs in complex samples.

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Abstract Reference & Short Personal Biography of Presenting Author

References:

1 Darrouzain F, Bian S, Desvignes C, et al. Therapeutic drug monitoring, 2017, 39(4): 316-321.

2 Wang X, Xia D, Han H, et al. Analytica chimica acta, 2018, 1017: 57-65.

Dr. Zhengjin Jiang received his PhD degree in the Institute of Elemento-Organic Chemistry, Nankai University in 2001. After graduation, he worked for one year in Unimicro (Tianjin) Technologies, Inc, followed as postdoctoral researcher or research fellow in The University of Tuebingen in Germany, King‘s College London, Pfizer (Sandwich) Research Centre, Novartis Horsham Research Centre, respectively. In 2011, he returned to China and became a full professor of pharmacy at Jinan University, China. His research has been focused on separation science and their applications in pharmaceutical analysis. So far, he has published over 100 scientific publications in international peer-reviewed journals and given more than 30 oral presentations at international/domestic conferences (including 20 keynotes). He is also the holder of 7 patens. He also served as chair of the 27th International Symposium on Pharmaceutical and Biomedical Analysis in 2016, permeant board member of steering committee of PBA and international scientific committee member of ISC2018, PBA2018 and PBA2019, APA2017 etc.. Current, he serves as editorial board member of Journal of Pharmaceutical and Biomedical Analysis, Chinese Journal of Pharmaceutical Analysis, Journal of Pharmaceutical Analysis etc.