Document Type
Article
Publication Date
11-2025
Keywords
AAV full capsid separation, membrane chromatography, MMAEX ligand
Abstract
A multi-modal anion exchange ligand 2-methyl-phenylimidazole has been successfully functionalized on highly porous electrospun regenerated cellulose membrane substrate for the separation of full and empty adeno-associated viral (AAV) capsids. The functionalized membrane has an average pore size of 0.5 mu m and exhibits both charge and hydrophobic functionality. The ligand is able to distinguish the subtle physio-chemical differences between the full and empty viral capsids. The multi-modal anion exchange membrane is able to separate the full capsids from affinity-captured mammalian AAV2 using both gradient and two-step elution methods with superior performance. A full capsid recovery of 72.9% at 85.3% purity with gradient elution, or 70.3% recovery at 92.2% purity with two-step elution can be achieved at significantly higher viral capsid loading of approximate to 0.5-1.3 x 1014 particles mL-1 of membrane volume compared to previous studies. Moreover, AAV2 capsids demonstrate similar transduction efficiency before and after the purification with the functionalized membrane.
Citation
X. Hao, S. R. Wickramasinghe, and X. Qian, “ Fabrication of Multimodal Anion Exchange Membrane for Chromatographic Purification of Full Adeno-Associated Viral Capsids.” Adv. Mater. Interfaces 12, no. 22 (2025): e00571. https://doi.org/10.1002/admi.202500571
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Comments
Web of Science
Wiley