Mass spectrometric identification of proteins enhanced by the atomic force microscopy immobilization surface

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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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Kaysheva, A. L., Frantsuzov, P. A., Kopylov, A. T., Pleshakova, T. O., Stepanov, A. A., Malsagova, K. A., … Ivanov, Y. D. (2021). Mass spectrometric identification of proteins enhanced by the atomic force microscopy immobilization surface. International Journal of Molecular Sciences, 22(1), 1–13. https://doi.org/10.3390/ijms22010431

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