Lectin-Glycan-Mediated Nanoparticle Docking as a Step toward Programmable Membrane Catalysis and Adhesion in Synthetic Protocells

Vincent Mukwaya, Peipei Zhang, Heze Guo, Auphedeous Yinme Dang-i, Qiangqiang Hu, Mei Li, Stephen Mann, Hongjing Dou*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

20 Citations (Scopus)
138 Downloads (Pure)


The spontaneous assembly of nanoscale building blocks into continuous semipermeable membranes is a key requirement for the structuration of synthetic protocells. Engineering the functionality and programmability of these building units provides a step toward more complex cell-like entities with adaptive membrane properties. Inspired by the central role of protein (lectin)–carbohydrate interactions in cellular recognition and adhesion, we fabricate semipermeable polysaccharide–polymer microcapsules (polysaccharidosomes) with intrinsic lectin-binding properties. We employ amphiphilic polysaccharide–polymer membrane building blocks endowed with intrinsic bio-orthogonal lectin–glycan recognition sites to facilitate the reversible noncovalent docking of functionalized polymer or zeolitic nanoparticles on the polysaccharidosomes. We show that the programmed attachment of enzyme-loaded nanoparticles gives rise to a membrane-gated spatially localized cascade reaction within the protocells due to the thermoresponsiveness of the polysaccharidosome membrane, and we demonstrate that extended closely packed networks are produced via reversible lectin-mediated adhesion between the protocells. Our results provide a step toward nanoscale engineering of bioinspired cell-like materials and could have longer-term applications in synthetic virology, protobiology, and microbiosensor and microbioreactor technologies.
Original languageEnglish
Pages (from-to)7899–7910
Number of pages12
JournalACS Nano
Issue number7
Early online date8 May 2020
Publication statusPublished - 28 Jul 2020

Structured keywords

  • Bristol BioDesign Institute


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