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Molecularly Imprinted Polymer Nanogels for Protein Recognition: Direct Proof of Specific Binding Sites by Solution STD and WaterLOGSY NMR Spectroscopies
Author(s) -
Mier Alejandra,
Maffucci Irene,
Merlier Franck,
Prost Elise,
Montagna Valentina,
RuizEsparza Guillermo U.,
Bonventre Joseph V.,
Dhal Pradeep K.,
Tse Sum Bui Bernadette,
Sakhaii Peyman,
Haupt Karsten
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202106507
Subject(s) - epitope , molecularly imprinted polymer , molecular imprinting , linear epitope , peptide , chemistry , molecular recognition , imprinting (psychology) , biophysics , epitope mapping , target protein , combinatorial chemistry , microbiology and biotechnology , biochemistry , antigen , selectivity , biology , molecule , gene , genetics , organic chemistry , catalysis
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.