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Covalent Protein Immobilization onto Muscovite Mica Surface with a Photocrosslinker

Institute of Biomedical Chemistry, Pogodinskaya st., 10, 119121 Moscow, Russia
Author to whom correspondence should be addressed.
Minerals 2020, 10(5), 464;
Received: 31 March 2020 / Revised: 29 April 2020 / Accepted: 14 May 2020 / Published: 20 May 2020
Muscovite mica with an amino silane-modified surface is commonly used as a substrate in atomic force microscopy (AFM) studies of biological macromolecules. Herein, the efficiency of two different protein immobilization strategies employing either (N-hydroxysuccinimide ester)-based crosslinker (DSP) or benzophenone-based photoactivatable crosslinker (SuccBB) has been compared using AFM and mass spectrometry analysis. Two proteins with different physicochemical properties—human serum albumin (HSA) and horseradish peroxidase enzyme protein (HRP)—have been used as model objects in the study. In the case of HRP, both crosslinkers exhibited high immobilization efficiency—as opposed to the case with HSA, when sufficient capturing efficiency has only been observed with SuccBB photocrosslinker. The results obtained herein can find their application in commonly employed bioanalytical systems and in the development of novel highly sensitive chip-based diagnostic platforms employing immobilized proteins. The obtained data can also be of interest for other research areas in medicine and biotechnology employing immobilized biomolecules. View Full-Text
Keywords: muscovite mica; atomic force microscopy; crosslinker; protein immobilization muscovite mica; atomic force microscopy; crosslinker; protein immobilization
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Valueva, A.A.; Shumov, I.D.; Kaysheva, A.L.; Ivanova, I.A.; Ziborov, V.S.; Ivanov, Y.D.; Pleshakova, T.O. Covalent Protein Immobilization onto Muscovite Mica Surface with a Photocrosslinker. Minerals 2020, 10, 464.

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