Universal proteomics sample preparation is challenging because of the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for nonspecific immobilization on microparticles by protein aggregation capture. To demonstrate the general applicability of this mechanism, we analyzed phosphoproteomes, tissue proteomes, and interaction proteomes as well as dilute secretomes. The findings present a practical, sensitive and cost-effective proteomics sample preparation method.
Keywords: Affinity proteomics; Automation; Mass Spectrometry; Phosphoproteome; Protein Denaturation*; Secretome; magnetic beads; microparticles; protein aggregation; sample preparation.
© 2019 Batth et al.