Mass Spectrometry-Based Protein Sequencing Platforms

Abstract

The amino-terminal sequencing methods was first introduced by the stepwise degradation of peptides applied in 1930 by Abderhalden and Brockmann (1930), which was improved by Pehr Edman (1949) in 1949. Until mid 1980s, the “Edman degradation” procedure had been used to determine the sequence of the N-terminal 30–40 amino acid residues in a protein routinely. The term “proteome”, linguistically equivalent to the concept of genome, was coined in 1994 to describe the complete set of proteins that is expressed according to the genome information and modified following expression in a lifetime of cells (Nature 1999). A simultaneous, high-throughput sequencing for more than thousands of peptides/proteins in complex biological samples had not been possible until both soft ionizations for biological molecules (MALDI, ESI etc.) (Tanaka et al. 1988; Karas and Hillenkamp 1988; Yamashita and Fenn 1984; Fenn et al. 1989) and mass spectrometry (MS)-driven sequencing technologies have been developed. This MS- based proteomics has dramatically revolutionized the sequencing and identification of proteins/peptides in complex biological samples. Clinical proteomics is nowadays a science to understand dynamic protein-centric biomolecular networks spatially and temporally in diseased cells and organs.