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dc.contributor.authorBhakta, Snehasis
dc.contributor.authorSeraji, Mohammad Saiful Islam
dc.contributor.authorSuib, Steven L.
dc.contributor.authorRusling, James F.
dc.date.accessioned2018-09-20T16:01:01Z
dc.date.available2018-09-20T16:01:01Z
dc.date.issued2015-12-30
dc.identifier.citationBhakta, Snehasis; Seraji, Mohammad Saiful Islam; Suib, Steven L. Rusling, James F. (2015). Antibody-like biorecognition sites for proteins from surface imprinting on nanoparticles. ACS Applied Materials & Interfaces 7 (51), 28197-28206
dc.identifier.issn1944-8244,1944-8252
dc.identifier.urihttp://hdl.handle.net/10379/10428
dc.description.abstractNatural antibodies are used widely for important applications such as biomedical analysis, cancer therapy, and directed drug delivery, but they are expensive and may have limited stability. This study describes synthesis of antibody-like binding sites by molecular imprinting on silica nanoparticles (SiNP) using a combination of four organosilane monomers with amino acid-like side chains providing hydrophobic, hydrophilic, and H-bonding interactions with target proteins. This approach provided artificial antibody (AA) nanoparticles with good selectivity and specificity to binding domains on target proteins in a relatively low-cost synthesis. The AAs were made by polymer grafting onto SiNPs for human serum albumin (HSA) and glucose oxidase (GOx). Binding affinity, selectivity, and specificity was compared to several other proteins using adsorption isotherms and surface plasmon resonance (SPR). The Langmuir-Freundlich adsorption model was used to obtain apparent binding constants (K-LF) from binding isotherms of HSA (6.7 X 10(4)) and GOx (4.7 X 10(4)) to their respective AAs. These values were 4-300 fold larger compared to a series of nontemplate proteins. SPR binding studies of AAs with proteins attached to a gold surface confirmed good specificity and revealed faster binding for the target proteins compared to nontarget proteins. Target proteins retained their secondary structures upon binding. Binding capacity of AA(HSA) for HSA was 5.9 mg HSA/g compared to 1.4 mg/g for previously report imprinted silica beads imprinted with poly(aminophenyl)boronic acid. Also, 90% recovery for HSA spiked into 2% calf serum was found for AA(HSA).
dc.publisherAmerican Chemical Society (ACS)
dc.relation.ispartofACS Applied Materials & Interfaces
dc.subjectmolecular imprinting
dc.subjectsilica nanoparticles
dc.subjecthuman serum albumin (hsa)
dc.subjectsurface plasmon resonance (spr)
dc.subjectlangmuir-freundlich adsorption
dc.subjectimmunosorbent-assay elisa
dc.subjectresistive-pulse measurements
dc.subjectbovine serum-albumin
dc.subjectsol-gel process
dc.subjectnanopipettes detection
dc.subjectmonoclonal-antibodies
dc.subjectinteraction forces
dc.subjectcrystal-structure
dc.subjectrecognition
dc.subjecthemoglobin
dc.titleAntibody-like biorecognition sites for proteins from surface imprinting on nanoparticles
dc.typeArticle
dc.identifier.doi10.1021/acsami.5b11650
dc.local.publishedsourcehttp://europepmc.org/articles/pmc4749148?pdf=render
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