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 …