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Thin Films of Lanthanide Stearates as Modifiers of the Q-Sense Device Sensor for Studying Insulin Adsorption

[Image: see text] This article presents new possibilities of using thin films of lanthanide stearates as sorbent materials. Modification of the Q-sense device resonator with monolayers of lanthanide stearates by the Langmuir–Schaeffer method made it possible to study the process of insulin protein a...

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Detalles Bibliográficos
Autores principales: Ladikan, Olga, Silyavka, Elena, Mitrofanov, Andrei, Laptenkova, Anastasia, Shilovskikh, Vladimir, Kolonitckii, Petr, Ivanov, Nikita, Remezov, Andrey, Fedorova, Anna, Khripun, Vassily, Pestova, Olga, Podolskaya, Ekaterina P., Sukhodolov, Nikolai G., Selyutin, Artem A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9330115/
https://www.ncbi.nlm.nih.gov/pubmed/35910105
http://dx.doi.org/10.1021/acsomega.1c07300
Descripción
Sumario:[Image: see text] This article presents new possibilities of using thin films of lanthanide stearates as sorbent materials. Modification of the Q-sense device resonator with monolayers of lanthanide stearates by the Langmuir–Schaeffer method made it possible to study the process of insulin protein adsorption on the surface of new thin-film sorbents. The resulting films were also characterized by compression isotherms, chemical analysis, scanning electron microscopy, and mass spectrometry. The transition of stearic acid to salt was recorded by IR spectroscopy. Using the LDI MS method, the main component of thin films, lanthanide distearate, was established. The presence of Eu(2+) in thin films was revealed. In the case of europium stearate, the maximum value of insulin adsorption was obtained, −1.67·10(−10) mole/cm(2). The findings suggest the possibility of using thin films of lanthanide stearates as a sorption material for the proteomics determination of the quantitative protein content in complex fluid systems by specific adsorption on modified surfaces and isolation of such proteins from complex mixtures.