Oxytocin-Selective Nanogel Antibody Mimics

Rashmi Mahajan,Jesper G Wiklander,Subramanian Suriyanarayanan,Ian A Nicholls,Teodor Aastrup,Börje Sellergren,Gustaf D Olsson

doi:10.3390/ijms23052534

Abstract

Oxytocin imprinted polymer nanoparticles were synthesized by glass bead supported solid phase synthesis, with NMR and molecular dynamics studies used to investigate monomer–template interactions. The nanoparticles were characterized by dynamic light scattering, scanning- and transmission electron microscopy and X-ray photoelectron spectroscopy. Investigation of nanoparticle-template recognition using quartz crystal microbalance-based studies revealed sub-nanomolar affinity, kd ≈ 0.3 ± 0.02 nM (standard error of the mean), comparable to that of commercial polyclonal antibodies, kd ≈ 0.02–0.2 nM.

Highlights

Sellergren, B.; Nicholls, I.A.The selective detection of proteins and peptides is critical for the function of many clinical diagnostics and therapeutics, and for numerous processes in the pharmaceutical and biotechnology industries [1,2]
The polymer composition used for synthesis of oxytocin imprinted nanoparticles (O-NPs) was adopted from previous studies where similar mixtures of polar and hydrophobic monomers were successfully used for imprinting of peptides and proteins [17,21]
To gain further insight into pre-polymerization interactions, molecular dynamics studies were performed for a system mimicking the mixture used to synthesize O-NPs (Figure S12)

Summary

Introduction

Sellergren, B.; Nicholls, I.A.The selective detection of proteins and peptides is critical for the function of many clinical diagnostics and therapeutics, and for numerous processes in the pharmaceutical and biotechnology industries [1,2]. Antibodies are often used for protein detection due to the high specificities and selectivities they can display [3]; their production can be time-consuming and resource demanding [4]. Their limited chemical and physical stabilities often lead to short shelf-lives and the need for refrigerated transport and storage [5]. The initial demonstration of antibody-like ligand specificities and selectivities in small molecule imprinted polymers [13] and the physical and chemical stabilities of these materials [14] has helped drive the search for new polymer compositions, design strategies, formats and synthesis methods suitable for use in the molecular imprinting of biomacromolecules [15,16]. The subsequent development of molecularly imprinted polymer synthesis using biomacromolecular templates immobilized on the surfaces of flat substrates [19] and particles, e.g., beads [20]

Methods

Results

Conclusion