Once introduced into a biological environment such as blood, nanoparticles (NPs) tend to adsorb proteins onto their surface creating a layer known as the protein corona, this ultimately changes their surface identity. Furthermore, it is well known that carbohydrates are overexpressed on the surface of cells, and are involved in many biological processes such as cell-cell recognition. Glycopolymers are synthetic polymers bearing carbohydrate units which maintain their binding efficiency with glycan binding proteins, such as lectins, thus they gained attention in recent decades as promising candidates to study carbohydrate-protein interactions. This work aims in the preparation of mannosylated nanoparticles for the evaluation of targeted protein affinity. Polymerization-induced self-assembly (PISA) in disperse media was employed as polymerization technique allowing the in simultaneous chain extension and in situ self-assembly of a glycosylated macroinitiator. Herein, we describe the novel synthesis and analysis of glycosylated NPs utilizing single electron transfer living radical polymerization induced self-assembly (SET-LR-PISA). Poly(ethylene glycol methacrylate)-statistical-poly(propalgyl methacrylate) (PEGMA-s-PPgMA) was obtained by conventional atom-transfer copolymerization (ATRP), and was subsequently glycosylated via copper catalysed alkyne-azide cycloaddition (CuAAC), utilising two different azo-mannosides derivatives with differing linker lengths. The glycosylated macroinitiator was then chain extended with 2-hydroxypropyl methacrylate (HPMA) via SET-LRP, which induced self-assembly, yielding mannosylated NPs. Manosylated NPs were analysed by dynamic light scattering (DLS) and transmission electron microscopy (TEM) in order to determine their size and morphologies.

Glycosylated nanoparticle by SET-LRP PISA

ACS Spring Meeting 2021

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