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Bioorthogonal tuning of nanosurface opsonisation via click coupling of a complement fusion protein inhibitor

Lookup NU author(s): Professor Moein MoghimiORCiD

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).

Abstract

This journal is © The Royal Society of Chemistry, 2026. Complement opsonisation contributes to immune clearance of nanopharmaceuticals, but complement activation has some undesirable effects. Herein, we show that tethering the fusion complement receptor 2-complement receptor 1 (CR2-CR1) regulator to cross-linked iron oxide nanoworms via a PEG spacer and copper-free click chemistry overcomes complement opsonisation. Furthermore, CR2-CR1-conjugated nanoworms reduce complement opsonisation of unmodified nanoparticles.

Publication metadata

Author(s): Jacques S, Gaikwad H, Pillatzke J, Moghimi SM, Simberg D

Publication type: Article

Publication status: Published

Journal: Chemical Communications

Year: 2026

Pages: Epub ahead of print

Online publication date: 09/06/2026

Acceptance date: 04/06/2026

Date deposited: 23/06/2026

ISSN (print): 1359-7345

ISSN (electronic): 1364-548X

Publisher: Royal Society of Chemistry

URL: https://doi.org/10.1039/d6cc00733c

DOI: 10.1039/d6cc00733c

Data Access Statement: All data supporting this article are present in the paper and/or the supplementary information (SI). Supplementary information: experimental procedures and 1H-NMR data for MTz-PEG3400-COOH are included in SI. See DOI: https://doi.org/10.1039/d6cc00733c.

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