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Mass Spectrometric Identification of BSA Covalently Captured onto a Chip for Atomic Force Microscopy.


ABSTRACT: Mass spectrometry (MS) is one of the main techniques for protein identification. Herein, MS has been employed for the identification of bovine serum albumin (BSA), which was covalently immobilized on the surface of a mica chip intended for investigation by atomic force microscopy (AFM). For the immobilization, two different types of crosslinkers have been used: 4-benzoylbenzoic acid N-succinimidyl ester (SuccBB) and dithiobis(succinimidyl propionate) (DSP). According to the data obtained by using an AFM-based molecular detector, the SuccBB crosslinker was more efficient in BSA immobilization than the DSP. The type of crosslinker used for protein capturing has been found to affect the results of MS identification. The results obtained herein can be applied in the development of novel systems intended for the highly sensitive analysis of proteins with molecular detectors.

SUBMITTER: Gordeeva AI 

PROVIDER: S-EPMC10219506 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature

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Mass Spectrometric Identification of BSA Covalently Captured onto a Chip for Atomic Force Microscopy.

Gordeeva Arina I AI   Valueva Anastasia A AA   Ershova Maria O MO   Rybakova Elizaveta E EE   Shumov Ivan D ID   Kozlov Andrey F AF   Ziborov Vadim S VS   Zavialova Maria G MG   Zgoda Victor G VG   Ivanov Yuri D YD   Archakov Alexander I AI   Pleshakova Tatyana O TO  

International journal of molecular sciences 20230519 10


Mass spectrometry (MS) is one of the main techniques for protein identification. Herein, MS has been employed for the identification of bovine serum albumin (BSA), which was covalently immobilized on the surface of a mica chip intended for investigation by atomic force microscopy (AFM). For the immobilization, two different types of crosslinkers have been used: 4-benzoylbenzoic acid N-succinimidyl ester (SuccBB) and dithiobis(succinimidyl propionate) (DSP). According to the data obtained by usin  ...[more]

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