Specifications table

Subject area	Biology
More specific subject area	Biochemistry, immuno-MALDI MS analysis, protein detection
Type of data	Spectra, figures, tables
How data was acquired	Proteins identification was carried out using Autoflex III time-of-flight mass-spectrometer (Bruker, Germany), equipped with nitrogen laser with emission wavelength of 337 nm. To control efficiency of working AFM-chip surfaces enrichment, NTEGRA Prima atomic force microscope by NT-MDT (Zelenograd, Russia), AppNano cantilevers (USA), ACSTA model were employed.
Data format	Raw, filtered, analyzed
Experimental factors	To carry out specific enrichment of HCVcoreAg the AFM-chip with immobilized aptamers was incubated in blood serum samples. Subsequently, the AFM-chip was washed with deonized water and dried in presence of nitrogen flow. The trypsin digestion on the surface of AFM chip was used.
Experimental features	Mica with maximum surface elevation difference of up to 0.5 nm was used as AFM-chip. Four zones with immobilized aptamers were formed on the surfaces of working and control AFM-chips. Working AFM-chips were incubated in blood serum samples containing HCV RNA by PCR whereas, control AFM-chips were incubated in blood serum samples from healthy volunteers.
Data source location	Moscow, Russia
Data accessibility	The mass spectrometry data have been deposited to the web-site IBMC http://www.ibmc.msk.ru/content/lab_nanobiotech/MALDI_MS.zip
Related research article	Ivanov YD, Kaysheva AL, Frantsuzov PA, Pleshakova TO, Krohin NV, Izotov AA, Shumov ID, Uchaikin VF, Konev VA, Ziborov VS, Archakov AI. Detection of hepatitis C virus core protein in serum by atomic force microscopy combined with mass spectrometry. Int J Nanomedicine. https://doi.org/10.2147/IJN.S71776.