Dummy Imprinted Proteins as Receptors for Bioinorganic Sorbent

A procedure is developed for preparing a selective bioinorganic adsorbent based on silicon dioxide particles modified with an imprinted protein (IPs). Bovine serum albumin served as the matrix protein molecule. The imprinting process was carried out in the presence of several template molecules—coumarin, 4-hydroxycoumarin, quercetin, and 5,7-dimethoxycoumarin—which acted as dummy templates of the mycotoxin ZEN. To pre-evaluate the feasibility of replacing ZEN with dummy templates and to determine the optimal concentration of the template molecules for IP synthesis, methods of computational chemistry were used, including molecular docking and molecular dynamics. Surface premodification of silicon dioxide particles proved essential for synthesizing IP-based sorbents. The resulting bioinorganic adsorbents demonstrated ability of extracting template molecules through solid-phase extraction from model solutions: coumarin (Q = 2.0 mg/g), 4-hydroxycoumarin (Q = 1.2 mg/g), quercetin (Q = 0.8 mg/g), 5,7-dimethoxycoumarin (Q = 2.2 mg/g), and ZEN from a wheat extract (Q = 4.79 mg/g, IF = 2.45). Zearalenone adsorption isotherms were constructed for IP-modified sorbents synthesized using different dummy templates. The cytotoxicity of the IPs was studied and their biosafety was assessed using the AGREEMIP tool.

Authors

Institutions

Publication Details

Journal
Journal of Analytical Chemistry
Published
2025-10-01
DOI
https://doi.org/10.1134/s106193482570087x
Primary Topic
Analytical chemistry methods development
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Dummy Imprinted Proteins as Receptors for Bioinorganic Sorbent

Pavel S. Pidenko, Polina M. Ilicheva, Daria V. Tsyupka, Kirill Yu. Presnyakov et al.
Journal of Analytical Chemistry
Analytical chemistry methods development
article

Dummy Imprinted Proteins as Receptors for Bioinorganic Sorbent

Pavel S. Pidenko, Polina M. Ilicheva, Daria V. Tsyupka, Kirill Yu. Presnyakov, Н. А. Бурмистрова, Ilya E. Menyailo
article en

Abstract

A procedure is developed for preparing a selective bioinorganic adsorbent based on silicon dioxide particles modified with an imprinted protein (IPs). Bovine serum albumin served as the matrix protein molecule. The imprinting process was carried out in the presence of several template molecules—coumarin, 4-hydroxycoumarin, quercetin, and 5,7-dimethoxycoumarin—which acted as dummy templates of the mycotoxin ZEN. To pre-evaluate the feasibility of replacing ZEN with dummy templates and to determine the optimal concentration of the template molecules for IP synthesis, methods of computational chemistry were used, including molecular docking and molecular dynamics. Surface premodification of silicon dioxide particles proved essential for synthesizing IP-based sorbents. The resulting bioinorganic adsorbents demonstrated ability of extracting template molecules through solid-phase extraction from model solutions: coumarin (Q = 2.0 mg/g), 4-hydroxycoumarin (Q = 1.2 mg/g), quercetin (Q = 0.8 mg/g), 5,7-dimethoxycoumarin (Q = 2.2 mg/g), and ZEN from a wheat extract (Q = 4.79 mg/g, IF = 2.45). Zearalenone adsorption isotherms were constructed for IP-modified sorbents synthesized using different dummy templates. The cytotoxicity of the IPs was studied and their biosafety was assessed using the AGREEMIP tool.

Journal of Analytical ChemistryVol. 80(10)
Saratov State University (RU)
Openalex Percentile: Top 66%
Analytical chemistry methods development
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.