Complementary IMAC enrichment methods for HLA-associated phosphopeptide identification by mass spectrometry.

ABSTRACT: Phosphorylation events within cancer cells often become dysregulated, leading to oncogenic signaling and abnormal cell growth. Phosphopeptides derived from aberrantly phosphorylated proteins that are presented on tumors and not on normal tissues by human leukocyte antigen (HLA) class I molecules are promising candidates for future cancer immunotherapies, because they are tumor specific and have been shown to elicit cytotoxic T cell responses. Robust phosphopeptide enrichments that are suitable for low input amounts must be developed to characterize HLA-associated phosphopeptides from clinical samples that are limited by material availability. We present two complementary mass spectrometry-compatible, iron(III)-immobilized metal affinity chromatography (IMAC) methods that use either nitrilo

SUBMITTER: Abelin JG 

PROVIDER: S-EPMC4640213 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature