2022
DOI: 10.1039/d2nr03898f
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How an ACE2 mimicking epitope-MIP nanofilm recognizes template-related peptides and the receptor binding domain of SARS-CoV-2

Abstract: Here we aim to the mechanistic understanding of the formation of epitope-imprinted polymer nanofilms using non-terminal peptide sequence, i.e. the peptide GFNCYFP (G485 to P491) of SARS-CoV-2 receptor binding domain...

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Cited by 3 publications
(2 citation statements)
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“…The MIP generation based on this monomer could integrate epitope imprinting, surface imprinting and oriented template immobilization in a microarray format. The latter was achieved by microspotting first the peptide epitopes onto the gold surface of the SPRi biochip, which enabled the adjustment of the optimal GFNCYFPLQ peptide SARS-CoV-2 spike protein RBD SPRi 1.6 [18] GFNCYFP peptide SARS-CoV-2 spike protein RBD SPRi 2.2 [18] GFNCYFP peptide SARS-CoV-2 spike protein RBD SWV 57.6 [43] Cytochrome C Cytochrome C CV 10,000 [31] AYLKKATNE peptide Cytochrome C FL 8,540 [44] Transferrin Transferrin SWV 500 [37] HAS HSA CV 2,800 [19] VHLTP peptide Hemoglobin SWV 9.06 [b] [45]…”
Section: Discussionmentioning
confidence: 99%
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“…The MIP generation based on this monomer could integrate epitope imprinting, surface imprinting and oriented template immobilization in a microarray format. The latter was achieved by microspotting first the peptide epitopes onto the gold surface of the SPRi biochip, which enabled the adjustment of the optimal GFNCYFPLQ peptide SARS-CoV-2 spike protein RBD SPRi 1.6 [18] GFNCYFP peptide SARS-CoV-2 spike protein RBD SPRi 2.2 [18] GFNCYFP peptide SARS-CoV-2 spike protein RBD SWV 57.6 [43] Cytochrome C Cytochrome C CV 10,000 [31] AYLKKATNE peptide Cytochrome C FL 8,540 [44] Transferrin Transferrin SWV 500 [37] HAS HSA CV 2,800 [19] VHLTP peptide Hemoglobin SWV 9.06 [b] [45]…”
Section: Discussionmentioning
confidence: 99%
“…The results confirm, at least for this model case, the hypothesis that increased number of functionalities of the monomer may lead to higher affinity MIPs towards the target. The epitope-imprinted poly(Asp-UMB) proved to be superior in terms of its affinity towards RBD as compared with peptide epitope-imprinted polyscopoletin determined in the same conditions [18,43], although did not reach the K D value of 77 fM reported for RBD-imprinted poly(orto-phenylenediamine) based on EIS-based measurements [49]. The affinity is also outstanding when compared with the structurally similar polyscopoletin-based MIPs with K D values in the nanomolar range (Table 1.)…”
Section: Kinetics Of the Rbd Binding To The Epitope-imprinted Poly(as...mentioning
confidence: 99%