Mass Spectrometric Identification of Proteins Enhanced by the Atomic Force Microscopy Immobilization Surface |
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Authors: | Anna L Kaysheva Pavel A Frantsuzov Arthur T Kopylov Tatyana O Pleshakova Alexander A Stepanov Kristina A Malsagova Alexander I Archakov Yurii D Ivanov |
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Affiliation: | Institute of Biomedical Chemistry, 119121 Moscow, Russia; (P.A.F.); (A.T.K.); (T.O.P.); (A.A.S.); (K.A.M.); (A.I.A.); (Y.D.I.) |
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Abstract: | 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. |
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Keywords: | smooth chip mass spectrometry atomic force microscope protein detection |
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