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. 2022 Feb 25;23(5):2534.
doi: 10.3390/ijms23052534.

Oxytocin-Selective Nanogel Antibody Mimics

Rashmi Mahajan  1 , Subramanian Suriyanarayanan  1 , Gustaf D Olsson  1 , Jesper G Wiklander  1 , Teodor Aastrup  2 , Börje Sellergren  3 , Ian A Nicholls  1
Affiliations

Oxytocin-Selective Nanogel Antibody Mimics

Rashmi Mahajan et al. Int J Mol Sci. .

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.

Keywords: NMR; QCM; molecular dynamics; molecularly imprinted polymer; nanoparticle; oxytocin; peptide imprinting; plastic antibody; solid-phase synthesis.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Oxytocin.
Figure 2
Figure 2
Monomers used for the synthesis of oxytocin-molecularly imprinted nanoparticles.
Figure 3
Figure 3
(A) Transmission electron- and (B) scanning electron micrographs, and (C) DLS size distribution of oxytocin imprinted nanoparticles.
Figure 4
Figure 4
High resolution N1s XPS spectra; (A) ACA, (B) oxytocin-ACA, (C) O-NPs -oxytocin-ACA (CPS, counts per second).
Figure 5
Figure 5
Surface topography of the oxytocin immobilized ACA functionalized gold surface (A) before and (B) after binding with O-NPs, mapped using AFM in non-contact mode (Image size 10 × 10 µm).
Figure 6
Figure 6
Schematic representation of the immobilization of oxytocin on QCM chips for the detection of O-NPs; (A) LNB carboxyl surface activation by EDC/sulfo-NHS, (B) ACA immobilization, (C) ACA surface activation by EDC/sulfo-NHS, (D) oxytocin immobilization, (E) O-NPs binding.
Figure 7
Figure 7
QCM trace during immobilization of oxytocin on LNB carboxyl chip. (A) Carboxyl activation of LNB-chip by EDC/Sulfo-NHS; (B) ACA immobilization (2 injections); (C) deactivation by ethanolamine; (D) ACA activation by EDC/Sulfo-NHS; (E) oxytocin immobilization (three injections); (F) deactivation by ethanolamine.
Figure 8
Figure 8
(A) Resonant frequency changes observed for repeated injections of O-NPs on oxytocin functionalized LNB-carboxyl QCM chip, n = 8; (B) linear calibration curve for O-NPs binding to different modified surfaces, maximum change in resonant frequency as a function of concentration of O-NPs; (C) variation of kobs constant against concentrations of O-NPs to oxytocin surface. The kobs values were calculated using nonlinear curve fitting from the association part of the QCM binding curves.
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References

    1. Pandey S., Malviya G., Dvorakova M.C. Role of Peptides in Diagnostics. Int. J. Mol. Sci. 2021;22:8828. doi: 10.3390/ijms22168828. - DOI - PMC - PubMed
    1. Deb P.K., Al-Attraqchi O., Chandrasekaran B., Paradkar A., Tekade R.K. Basic Fundamentals of Drug Delivery. Academic Press; Cambridge, MA, USA: 2019. Protein/Peptide Drug Delivery Systems: Practical Considerations in Pharmaceutical Product Development; pp. 651–684.
    1. Borrebaeck C.A.K. Antibodies in Diagnostics—From Immunoassays to Protein Chips. Immunol. Today. 2000;21:379–382. doi: 10.1016/S0167-5699(00)01683-2. - DOI - PubMed
    1. Samaranayake H., Wirth T., Schenkwein D., Räty J.K., Ylä-Herttuala S. Challenges in Monoclonal Antibody-Based Therapies. Ann. Med. 2009;41:322–331. doi: 10.1080/07853890802698842. - DOI - PubMed
    1. Wang W., Singh S., Zeng D.L., King K., Nema S. Antibody Structure, Instability, and Formulation. J. Pharm. Sci. 2007;96:1–26. doi: 10.1002/jps.20727. - DOI - PubMed

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