Ivan A. Reshetnik
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Ivan A. Reshetnik has a total of 16 co-authors. Here are the top co-authors by number of shared publications:
- Natalia A. Burmistrova
Institute of Chemistry, Saratov State University, Saratov 410012, Russia
4 shared publications - Pavel S. Pidenko
Institute of Chemistry, Saratov State University, Saratov, Russia
4 shared publications - Polina M. Ilicheva
Institute of Chemistry, Saratov State University, Saratov, Russia
4 shared publications - Kirill Yu Presnyakov
Institute of Chemistry, Saratov State University, Saratov 410012, Russia
3 shared publications - Michail Vladimirovich Pozharov
Institute of Chemistry, Saratov State University, Saratov, Russia
3 shared publications - Daniil D. Drozd
Institute of Chemistry, Saratov State University, Saratov, Russia
2 shared publications
Latest Publications
- Open Access
Toward Rational Design of Imprinted Proteins Based on Albumins: Computational and Experimental Studies
Imprinted proteins (IPs) are promising materials for producing artificial alternatives to natural recognition systems (antibodies, aptamers, etc.) due to their high sorption properties and specificity. However, contemporary understanding of the imprinting process at the atomic level is rather limited, which hinders the rational design of more efficient IPs. In this paper, we use computational modeling to provide a description of fundamental principles of protein imprinting at the atomic level. We have modeled several potential associates between the protein matrix and template molecules that form during the imprinting process up to the addition of the cross-linking agent. We used bovine serum albumin (BSA) as the protein matrix and 4-hydroxycoumarin (4–HC) as a molecular template. In combination with computational modeling, extensive experimental analyses including isothermal titration calorimetry (ITC) and NMR spectroscopic methods (1H NMR and diffusion-ordered NMR spectroscopy (DOSY)) were used to evaluate the potential efficiency of imprinted BSA. This study represents a step toward the future rational in silico design of IPs.
Open AccessToward Rational Design of Imprinted Proteins Based on Albumins: Computational and Experimental Studies
Imprinted proteins (IPs) are promising materials for producing artificial alternatives to natural recognition systems (antibodies, aptamers, etc.) due to their high sorption properties and specificity. However, contemporary understanding of the imprinting process at the atomic level is rather limited, which hinders the rational design of more efficient IPs. In this paper, we use computational modeling to provide a description of fundamental principles of protein imprinting at the atomic level. We have modeled several potential associates between the protein matrix and template molecules that form during the imprinting process up to the addition of the cross-linking agent. We used bovine serum albumin (BSA) as the protein matrix and 4-hydroxycoumarin (4–HC) as a molecular template. In combination with computational modeling, extensive experimental analyses including isothermal titration calorimetry (ITC) and NMR spectroscopic methods (1H NMR and diffusion-ordered NMR spectroscopy (DOSY)) were used to evaluate the potential efficiency of imprinted BSA. This study represents a step toward the future rational in silico design of IPs.
- Open Access
- 3 March 2026
- Published by MDPI AG in Biosensors
- Vol. 16 (3) , 149
Imprinted Proteins as a Receptor in Fluorescent Sensing Microplate Assay for Herbicide Determination
The manuscript describes an optical sensing microplate for the high-throughput screening of imidazolinone herbicides in soil extracts. As far as we know, imprinted proteins (IPs) specific to imidazolinone herbicides have not been synthesized and used as a recognition element for their solid-phase extraction before. Imprinted bovine serum albumin (BSA) and glucose oxidase (GOx) were synthesized in the presence of imazamox as a template and then these IPs were immobilized at the bottom of microplate wells. The sorption capacity (Q) of aminated silica nanoparticles modified by IPs (IP–BIS) was 6.38 mg g−1 while the imprinting factor () equaled 2.6. The concentration of imazamox was determined by a “turn-off” solid-phase assay using alloyed CdZnSeS/ZnS quantum dots (QDs) as a component of fluorescent substrate. Alloyed CdZnSeS/ZnS QDs were stabilized in an aqueous phase by positively charged cysteamine that, as far we know, had not been used as this type of ligand before. Our method allows for determining the concentration of imazamox in the range of 0.5–9.2 μg mL−1, with a limit of quantification limit of quantitation (LOQ) equal to 0.45 μg mL−1 The sensing microplate enables parallel detection of up to 96 samples containing herbicides using standard fluorescence microplate readers or smartphones. The paper describes how such sensing microplates can be used for the analysis of artificially contaminated soil samples. The proposed approach combines pre-concentration of analyte at the IPs with its subsequent determination on a single analytical platform, thus allowing for both highly sensitive determination in laboratory conditions and mass screening in the field.- 3 March 2026
- Published by MDPI AG in Biosensors
- Vol. 16 (3) , 149
Open AccessImprinted Proteins as a Receptor in Fluorescent Sensing Microplate Assay for Herbicide Determination
The manuscript describes an optical sensing microplate for the high-throughput screening of imidazolinone herbicides in soil extracts. As far as we know, imprinted proteins (IPs) specific to imidazolinone herbicides have not been synthesized and used as a recognition element for their solid-phase extraction before. Imprinted bovine serum albumin (BSA) and glucose oxidase (GOx) were synthesized in the presence of imazamox as a template and then these IPs were immobilized at the bottom of microplate wells. The sorption capacity (Q) of aminated silica nanoparticles modified by IPs (IP–BIS) was 6.38 mg g−1 while the imprinting factor () equaled 2.6. The concentration of imazamox was determined by a “turn-off” solid-phase assay using alloyed CdZnSeS/ZnS quantum dots (QDs) as a component of fluorescent substrate. Alloyed CdZnSeS/ZnS QDs were stabilized in an aqueous phase by positively charged cysteamine that, as far we know, had not been used as this type of ligand before. Our method allows for determining the concentration of imazamox in the range of 0.5–9.2 μg mL−1, with a limit of quantification limit of quantitation (LOQ) equal to 0.45 μg mL−1 The sensing microplate enables parallel detection of up to 96 samples containing herbicides using standard fluorescence microplate readers or smartphones. The paper describes how such sensing microplates can be used for the analysis of artificially contaminated soil samples. The proposed approach combines pre-concentration of analyte at the IPs with its subsequent determination on a single analytical platform, thus allowing for both highly sensitive determination in laboratory conditions and mass screening in the field. - 11 October 2025
- Published by Springer Nature in Analytical and Bioanalytical Chemistry
- Vol. 418 (2) , 587-596
A novel approach to determination of amino acids and cyclic heptapeptides using imprinted proteins
For the first time, imprinted proteins (IPs) were used as molecular recognition elements for determination of amino acids (arginine, Arg) and heptapeptides
- 11 October 2025
- Published by Springer Nature in Analytical and Bioanalytical Chemistry
- Vol. 418 (2) , 587-596
A novel approach to determination of amino acids and cyclic heptapeptides using imprinted proteins
For the first time, imprinted proteins (IPs) were used as molecular recognition elements for determination of amino acids (arginine, Arg) and heptapeptides
- Open Access
- 23 June 2025
- Published by Saratov State University in Izvestiya of Saratov University. Physics
- Vol. 25 (2)
Characterization of imprinted albumin by molecular modelling and spectroscopy
- 23 June 2025
- Published by Saratov State University in Izvestiya of Saratov University. Physics
- Vol. 25 (2)
Open AccessCharacterization of imprinted albumin by molecular modelling and spectroscopy