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Mier A, Maffucci I, Merlier F, et al. Molecularly Imprinted Polymer Nanogels for Protein Recognition: Direct Proof of Specific Binding Sites by Solution STD and WaterLOGSY NMR Spectroscopies. Angew Chem Int Ed Engl. 2021;60(38):20849-20857doi: 10.1002/anie.202106507.
Mier, A., Maffucci, I., Merlier, F., Prost, E., Montagna, V., Ruiz-Esparza, G. U., Bonventre, J. V., Dhal, P. K., Tse Sum Bui, B., Sakhaii, P., & Haupt, K. (2021). Molecularly Imprinted Polymer Nanogels for Protein Recognition: Direct Proof of Specific Binding Sites by Solution STD and WaterLOGSY NMR Spectroscopies. Angewandte Chemie (International ed. in English), 60(38), 20849-20857. https://doi.org/10.1002/anie.202106507
Mier, Alejandra, et al. "Molecularly Imprinted Polymer Nanogels for Protein Recognition: Direct Proof of Specific Binding Sites by Solution STD and WaterLOGSY NMR Spectroscopies." Angewandte Chemie (International ed. in English) vol. 60,38 (2021): 20849-20857. doi: https://doi.org/10.1002/anie.202106507
Mier A, Maffucci I, Merlier F, Prost E, Montagna V, Ruiz-Esparza GU, Bonventre JV, Dhal PK, Tse Sum Bui B, Sakhaii P, Haupt K. Molecularly Imprinted Polymer Nanogels for Protein Recognition: Direct Proof of Specific Binding Sites by Solution STD and WaterLOGSY NMR Spectroscopies. Angew Chem Int Ed Engl. 2021 Sep 13;60(38):20849-20857. doi: 10.1002/anie.202106507. Epub 2021 Aug 24. PMID: 34296498; PMCID: PMC8562893.
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Angew Chem Int Ed Engl. 2021 Sep 13;60(38):20849-20857. doi: 10.1002/anie.202106507. Epub 2021 Aug 24.

Molecularly Imprinted Polymer Nanogels for Protein Recognition: Direct Proof of Specific Binding Sites by Solution STD and WaterLOGSY NMR Spectroscopies.

Angewandte Chemie (International ed. in English)

Alejandra Mier, Irene Maffucci, Franck Merlier, Elise Prost, Valentina Montagna, Guillermo U Ruiz-Esparza, Joseph V Bonventre, Pradeep K Dhal, Bernadette Tse Sum Bui, Peyman Sakhaii, Karsten Haupt

Affiliations

  1. CNRS Enzyme and Cell Engineering Laboratory, Université de Technologie de Compiègne, Rue du Docteur Schweitzer, CS 60319, 60203, Compiègne Cedex, France.
  2. Divisions of Engineering in Medicine and Renal Medicine, Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, Boston, MA, 02115, USA.
  3. Division of Health Science and Technology, Harvard University-Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.
  4. US Early Development, Sanofi Global R&D, 153 Second Avenue, Waltham, MA, 02451, USA.
  5. R&D Global CMC Development-Synthetics-Early Development Frankfurt, Sanofi-Aventis (Deutschland) GmbH, Industriepark Hoechst, Frankfurt am Main, Germany.

PMID: 34296498 PMCID: PMC8562893 DOI: 10.1002/anie.202106507

Abstract

Molecularly imprinted polymers (MIPs) are tailor-made synthetic antibodies possessing specific binding cavities designed for a target molecule. Currently, MIPs for protein targets are synthesized by imprinting a short surface-exposed fragment of the protein, called epitope or antigenic determinant. However, finding the epitope par excellence that will yield a peptide "synthetic antibody" cross-reacting exclusively with the protein from which it is derived, is not easy. We propose a computer-based rational approach to unambiguously identify the "best" epitope candidate. Then, using Saturation Transfer Difference (STD) and WaterLOGSY NMR spectroscopies, we prove the existence of specific binding sites created by the imprinting of this peptide epitope in the MIP nanogel. The optimized MIP nanogel could bind the epitope and cognate protein with a high affinity and selectivity. The study was performed on Hepatitis A Virus Cell Receptor-1 protein, also known as KIM-1 and TIM-1, for its ubiquitous implication in numerous pathologies.

© 2021 Wiley-VCH GmbH.

Keywords: HAVCR-1; NMR; epitope; molecularly imprinted polymer; rational design

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