Self-oriented nanoparticles for site-selective immunoglobulin G recognition via epitope imprinting approach

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dc.authoridUzun, Lokman/0000-0002-3971-7725
dc.authoridCorman, Mehmet Emin/0000-0001-9062-4201
dc.authoridArmutcu, Canan/0000-0002-0920-2843
dc.contributor.authorCorman, Mehmet Emin
dc.contributor.authorArmutcu, Canan
dc.contributor.authorUzun, Lokman
dc.contributor.authorSay, Ridvan
dc.contributor.authorDenizli, Adil
dc.date.accessioned2025-03-23T19:41:51Z
dc.date.available2025-03-23T19:41:51Z
dc.date.issued2014
dc.departmentSinop Üniversitesi
dc.description.abstractMolecular imprinting is a polymerization technique that provides synthetic analogs for template molecules. Molecularly imprinted polymers (MIPs) have gained much attention due to their unique properties such as selectivity and specificity for target molecules. In this study, we focused on the development of polymeric materials with molecular recognition ability, so molecular imprinting was combined with miniemulsion polymerization to synthesize self-orienting nanoparticles through the use of an epitope imprinting approach. Thus, L-lysine imprinted nanoparticles (LMIP) were synthesized via miniemulsion polymerization technique. Immunoglobulin G (IgG) was then bound to the cavities that specifically formed for L-lysine molecules that are typically found at the C-terminus of the Fc region of antibody molecules. The resulting nanoparticles makes it possible to minimize the nonspecific interaction between monomer and template molecules. In addition, the orientation of the entire IgG molecule was controlled, and random imprinting of the IgG was prevented. The optimum conditions were determined for IgG recognition using the imprinted nanoparticles. The selectivity of the nanoparticles against IgG molecules was also evaluated using albumin and hemoglobin as competitor molecules. In order to show the self-orientation capability of imprinted nanoparticles, human serum albumin (HSA) adsorption onto both the plain nanoparticles and immobilized nanoparticles by anti-human serum albumin antibody (anti-HSA antibody) was also carried out. Due to anti-HSA antibody immobilization on the imprinted nanoparticles, the adsorption capability of nanoparticles against HSA molecules vigorously enhanced. It is proved that the oriented immobilization of antibodies was appropriately succeeded. (C) 2014 Elsevier B.V. All rights reserved.
dc.identifier.doi10.1016/j.colsurfb.2014.10.020
dc.identifier.endpage837
dc.identifier.issn0927-7765
dc.identifier.issn1873-4367
dc.identifier.pmid25454659
dc.identifier.scopus2-s2.0-84915818558
dc.identifier.scopusqualityQ1
dc.identifier.startpage831
dc.identifier.urihttps://doi.org/10.1016/j.colsurfb.2014.10.020
dc.identifier.urihttps://hdl.handle.net/11486/6662
dc.identifier.volume123
dc.identifier.wosWOS:000347580500103
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherElsevier
dc.relation.ispartofColloids and Surfaces B-Biointerfaces
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20250323
dc.subjectL-Lysine
dc.subjectMolecularly imprinted nanoparticles
dc.subjectSelf-orientation
dc.subjectAntibody
dc.subjectAnti-HSA
dc.titleSelf-oriented nanoparticles for site-selective immunoglobulin G recognition via epitope imprinting approach
dc.typeArticle

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