Incorporation of Novel Synthetic Glycolipids in Liposomal Nanoparticles Affects Opsonization and In Vivo Clearance
Mimicking cell membrane glycocalyx, saccharide modification of nanoparticles offers a potent means to regulate their in vivo fate. Here, we investigate how glycosylation (i.e., glucose, galactose, fructose, mannose, and N-acetylglucosamine) regulates liposomal nanoparticle interactions with plasma proteins and immune cells, which further determine their biodistribution and therapeutic efficacy. While fructose conferred the greatest enhancement in tumor cell uptake in vitro, N-acetylglucosamine-modified nanoparticles achieved the highest tumor accumulation and markedly attenuated systemic clearance in vivo, highlighting a pronounced disparity between in vitro and in vivo performance. The compromised in vivo efficacy of glycosylated nanoparticles was linked to significant clearance in blood, liver, and spleen, primarily mediated by blood monocytes, hepatic stellate cells, and splenic macrophages. Proteomics revealed that adsorption of immunoglobulin G (IgG) and complement C3 facilitates in vivo clearance of nanoparticles. Moreover, IgG deposition further promotes subsequent C3 binding. Notably, N-acetylglucosamine markedly mitigates IgG and C3 adsorption, leading to prolonged circulation and enhanced tumor accumulation and inhibition. Benefiting from glycosylation-regulated protein corona, doxorubicin-loaded N-acetylglucosamine-modified liposomal nanoparticles achieved superior antitumor efficacy compared with other glycosylated formulations. This study establishes a clear correlation between glycosyl ligand identity, protein corona composition, and in vivo performance, providing fundamental insights for rational design and clinical translation of glycosylated nanomedicines.
Authors
- Shijia Tao
- Wenshuai Han
- Katharina Landfester (ORCID: https://orcid.org/0000-0001-9591-4638)
- X.C. Li (ORCID: https://orcid.org/0000-0002-5981-2762)
- Volker Mailänder (ORCID: https://orcid.org/0000-0001-6583-8136)
- Daniel Crespy (ORCID: https://orcid.org/0000-0002-6023-703X)
- M Wang (ORCID: https://orcid.org/0009-0006-2920-0454)
- Yingjie Yu
- Xuehan Li (ORCID: https://orcid.org/0000-0002-7955-4705)
- Xiaoyan Fang
- Lemei Zhao
- Ying Qiu
- Luying Zhou
- Hao Fan
- Wenhua Yang
- Shuai Jiang
- Haiyang Zhang
- Yu Gao
- Xiangzhao Mao
Institutions
- Johannes Gutenberg University Mainz (DE)
- University Medical Center of the Johannes Gutenberg University Mainz (DE)
- Max Planck Institute for Polymer Research (DE)
- Qingdao National Laboratory for Marine Science and Technology (CN)
- Vidyasirimedhi Institute of Science and Technology (TH)
- Ocean University of China (CN)
Publication Details
- Journal
- Angewandte Chemie International Edition
- Published
- 2026-04-22
- DOI
- https://doi.org/10.1002/anie.202520837
- Primary Topic
- Glycosylation and Glycoproteins Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- Major Scientific and Technological Innovation Project of Shandong Province
- Fundamental Research Funds for the Central Universities