Investigation of Peptides for Molecular Recognition of C-Reactive Protein–Theoretical and Experimental Studies

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dc.contributor.authorSzot-Karpińska, Katarzyna
dc.contributor.authorKudła, Patryk
dc.contributor.authorOrzeł, Urszuła
dc.contributor.authorNarajczyk, Magdalena
dc.contributor.authorJönsson-Niedziółka, Martin
dc.contributor.authorPałys, Barbara
dc.contributor.authorFilipek, Sławomir
dc.contributor.authorEbner, Andreas
dc.contributor.authorNiedziółka-Jönsson, Joanna
dc.contributor.organizationInstitute of Physical Chemistry, Polish Academy of Sciencesen
dc.contributor.organizationUniversity of Warsawen
dc.contributor.organizationUniversity of Gdańsken
dc.contributor.organizationJohannes Kepler Universityen
dc.date.accessioned2023-12-20T10:29:55Z
dc.date.available2023-12-20T10:29:55Z
dc.date.issued2023
dc.description.abstractWe investigate the interactions between C-reactive protein (CRP) and new CRP-binding peptide materials using experimental (biological and physicochemical) methods with the support of theoretical simulations (computational modeling analysis). Three specific CRP-binding peptides (P2, P3, and P9) derived from an M13 bacteriophage have been identified using phage-display technology. The binding efficiency of the peptides exposed on phages toward the CRP protein was demonstrated via biological methods. Fibers of the selected phages/peptides interact differently due to different compositions of amino acid sequences on the exposed peptides, which was confirmed by transmission electron microscopy. Numerical and experimental studies consistently showed that the P3 peptide is the best CRP binder. A combination of theoretical and experimental methods demonstrates that identifying the best binder can be performed simply, cheaply, and fast. Such an approach has not been reported previously for peptide screening and demonstrates a new trend in science where calculations can replace or support laborious experimental techniques. Finally, the best CRP binder─the P3 peptide─was used for CRP recognition on silicate-modified indium tin oxide-coated glass electrodes. The obtained electrodes exhibit a wide range of operation (1.0–100 μg mL–1) with a detection limit (LOD = 3σ/S) of 0.34 μg mL–1. Moreover, the dissociation constant Kd of 4.2 ± 0.144 μg mL–1 (35 ± 1.2 nM) was evaluated from the change in the current. The selectivity of the obtained electrode was demonstrated in the presence of three interfering proteins. These results prove that the presented P3 peptide is a potential candidate as a receptor for CRP, which can replace specific antibodies.en
dc.description.sponsorshipPolish National Science Centre, 2017/26/D/ST5/00980en
dc.identifier.citationAnal. Chem. 2023, 95, 38, 14475–14483en
dc.identifier.doi10.1021/acs.analchem.3c03127
dc.identifier.urihttps://open.icm.edu.pl/handle/123456789/23413
dc.language.isoen
dc.publisherAmerican Chemical Societyen
dc.rightsUznanie autorstwa 4.0 Międzynarodowe*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectamidesen
dc.subjectcarbon fiberen
dc.subjectelectrodesen
dc.subjectpeptides and proteinsen
dc.subjectvirusesen
dc.titleInvestigation of Peptides for Molecular Recognition of C-Reactive Protein–Theoretical and Experimental Studiesen
dc.typearticleen
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