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Proteins embedded in membranes are critical for cell-cell communication, binding chemical messengers, and responding to environmental perturbation. Because cell surface proteins confer specific cellular functions and are easily accessible, they have been extensively targeted for drug design. In fact, plasma membrane proteins account for ~70% of all known drug targets. Profiling the cell surface protein expression of disease cells would provide protein targets for the design of therapeutic monoclonal antibodies or smallmolecule drugs. Analyses of cell surface proteome are commonly attempted by enriching plasma membrane proteins with sub-cellular fractionation, and then performing mass spectrometric analysis. Such studies reported relatively low cell surface protein identification percentages due to contamination with sub-cellular proteins from intracellular membranes. To overcome the problems of sub-cellular fractionation, researchers have studied the topological characteristics of cell surface proteins. Plasma membranes are physical barriers against non-membrane permeable compounds, which only encounter the extracellular domains of cell surface proteins. For instance, Sulfo-NHS-Biotin (biotin 3-sulfo-N-hydroxysuccinimide ester sodium salt) was used to selectively label cell surface proteins. Enrichment and ESI MS/MS protein profiling of biotinylated cell surface proteins from cell lysate resulted in a high cell surface protein identification percentage. Since the independent reports of the Sharpless and Medal

New Water-soluble Alkynylating Agent for Cell Surface Protein: Sulfosuccinimidyl 4-Pentynoate