Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Kaysheva, Anna L., Frantsuzov, Pavel A., Kopylov, Arthur T., Pleshakova, Tatyana O., Stepanov, Alexander A., Malsagova, Kristina A., Archakov, Alexander I., Ivanov, Yurii D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
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
_version_ 1783634557482827776
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
work_keys_str_mv AT kayshevaannal massspectrometricidentificationofproteinsenhancedbytheatomicforcemicroscopyimmobilizationsurface
AT frantsuzovpavela massspectrometricidentificationofproteinsenhancedbytheatomicforcemicroscopyimmobilizationsurface
AT kopylovarthurt massspectrometricidentificationofproteinsenhancedbytheatomicforcemicroscopyimmobilizationsurface
AT pleshakovatatyanao massspectrometricidentificationofproteinsenhancedbytheatomicforcemicroscopyimmobilizationsurface
AT stepanovalexandera massspectrometricidentificationofproteinsenhancedbytheatomicforcemicroscopyimmobilizationsurface
AT malsagovakristinaa massspectrometricidentificationofproteinsenhancedbytheatomicforcemicroscopyimmobilizationsurface
AT archakovalexanderi massspectrometricidentificationofproteinsenhancedbytheatomicforcemicroscopyimmobilizationsurface
AT ivanovyuriid massspectrometricidentificationofproteinsenhancedbytheatomicforcemicroscopyimmobilizationsurface