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Mass Spectrometric Identification of Proteins Enhanced by the Atomic Force Microscopy Immobilization Surface
An approach to highly-sensitive mass spectrometry detection of proteins after surface-enhanced concentrating has been elaborated. The approach is based on a combination of mass spectrometry and atomic force microscopy to detect target proteins. (1) Background: For this purpose, a technique for preli...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7795915/ https://www.ncbi.nlm.nih.gov/pubmed/33406706 http://dx.doi.org/10.3390/ijms22010431 |
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author | Kaysheva, Anna L. Frantsuzov, Pavel A. Kopylov, Arthur T. Pleshakova, Tatyana O. Stepanov, Alexander A. Malsagova, Kristina A. Archakov, Alexander I. Ivanov, Yurii D. |
author_facet | Kaysheva, Anna L. Frantsuzov, Pavel A. Kopylov, Arthur T. Pleshakova, Tatyana O. Stepanov, Alexander A. Malsagova, Kristina A. Archakov, Alexander I. Ivanov, Yurii D. |
author_sort | Kaysheva, Anna L. |
collection | PubMed |
description | An approach to highly-sensitive mass spectrometry detection of proteins after surface-enhanced concentrating has been elaborated. The approach is based on a combination of mass spectrometry and atomic force microscopy to detect target proteins. (1) Background: For this purpose, a technique for preliminary preparation of molecular relief surfaces formed as a result of a chemical or biospecific concentration of proteins from solution was developed and tested on several types of chip surfaces. (2) Methods: mass spectrometric identification of proteins using trailing detectors: ion trap, time of flight, orbital trap, and triple quadrupole. We used the electrospray type of ionization and matrix-assisted laser desorption/ionization. (3) Results: It is shown that when using locally functionalized atomically smooth surfaces, the sensitivity of the mass spectrometric method increases by two orders of magnitude as compared with measurements in solution. Conclusions: It has been demonstrated that the effective concentration of target proteins on specially prepared surfaces increases the concentration sensitivity of mass spectrometric detectors—time-of-flight, ion trap, triple quadrupole, and orbital ion trap in the concentration range from up to 10(−15) M. |
format | Online Article Text |
id | pubmed-7795915 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-77959152021-01-10 Mass Spectrometric Identification of Proteins Enhanced by the Atomic Force Microscopy Immobilization Surface Kaysheva, Anna L. Frantsuzov, Pavel A. Kopylov, Arthur T. Pleshakova, Tatyana O. Stepanov, Alexander A. Malsagova, Kristina A. Archakov, Alexander I. Ivanov, Yurii D. Int J Mol Sci Article An approach to highly-sensitive mass spectrometry detection of proteins after surface-enhanced concentrating has been elaborated. The approach is based on a combination of mass spectrometry and atomic force microscopy to detect target proteins. (1) Background: For this purpose, a technique for preliminary preparation of molecular relief surfaces formed as a result of a chemical or biospecific concentration of proteins from solution was developed and tested on several types of chip surfaces. (2) Methods: mass spectrometric identification of proteins using trailing detectors: ion trap, time of flight, orbital trap, and triple quadrupole. We used the electrospray type of ionization and matrix-assisted laser desorption/ionization. (3) Results: It is shown that when using locally functionalized atomically smooth surfaces, the sensitivity of the mass spectrometric method increases by two orders of magnitude as compared with measurements in solution. Conclusions: It has been demonstrated that the effective concentration of target proteins on specially prepared surfaces increases the concentration sensitivity of mass spectrometric detectors—time-of-flight, ion trap, triple quadrupole, and orbital ion trap in the concentration range from up to 10(−15) M. MDPI 2021-01-04 /pmc/articles/PMC7795915/ /pubmed/33406706 http://dx.doi.org/10.3390/ijms22010431 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kaysheva, Anna L. Frantsuzov, Pavel A. Kopylov, Arthur T. Pleshakova, Tatyana O. Stepanov, Alexander A. Malsagova, Kristina A. Archakov, Alexander I. Ivanov, Yurii D. Mass Spectrometric Identification of Proteins Enhanced by the Atomic Force Microscopy Immobilization Surface |
title | Mass Spectrometric Identification of Proteins Enhanced by the Atomic Force Microscopy Immobilization Surface |
title_full | Mass Spectrometric Identification of Proteins Enhanced by the Atomic Force Microscopy Immobilization Surface |
title_fullStr | Mass Spectrometric Identification of Proteins Enhanced by the Atomic Force Microscopy Immobilization Surface |
title_full_unstemmed | Mass Spectrometric Identification of Proteins Enhanced by the Atomic Force Microscopy Immobilization Surface |
title_short | Mass Spectrometric Identification of Proteins Enhanced by the Atomic Force Microscopy Immobilization Surface |
title_sort | mass spectrometric identification of proteins enhanced by the atomic force microscopy immobilization surface |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7795915/ https://www.ncbi.nlm.nih.gov/pubmed/33406706 http://dx.doi.org/10.3390/ijms22010431 |
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