RESUMO
Harvesting the low molecular weight (LMW) proteins from the cellular exudates is a big challenge for early disease detection. Here, we introduce a unique probe composed of surface-functionalized Fe2C NPs with different functional groups to harvest, identify and profile differentially expressed biomarker proteins. Three different functionalization of Fe2C NPs with Fe2C@NH2, Fe2C@COOH and Fe2C@PEG enabled to harvest 119 differentially expressed proteins from HeLa cell exudates. Among these proteins, 57 were LMW which 82.46 % were up-regulated and 17.54 % were down-regulated. The Fe2C@NH2 were able to separate 60S ribosomal proteins L7a, and L11, and leucine-rich repeat-containing protein 59. These proteins play a vital role in the maturation of large subunit ribosomal ribonucleic acid, mRNA splicing via spliceosome and cancer cell inhibitor, respectively. While, Fe2C@COOH identifies the 60S ribosomal protein types L7, 40S ribosomal protein S11, and 60S ribosomal protein L24. These proteins were important for large ribosomal subunit biogenesis, translational initiation, and assembly of large subunit precursor of pre-ribosome. Finally, the Fe2C@PEG extracted 40S ribosomal protein S2, splicing factor, arginine/serine-rich and 40S ribosomal protein S4, X isoform which were responsible for nonsense-mediated decay, oligodendrocyte differentiation and multicellular organism development. Thus, these results help us in defining oncogenic biomarkers for early disease detection.
