Photo-affinity labeling (PAL) in chemical proteomics: a handy tool to investigate protein-protein interactions (PPIs)

Authors
Murale, Dhiraj P.Hong, Seong CheolHaque, Md. MamunulLee, Jun-Seok
Issue Date
2017-06-24
Publisher
BIOMED CENTRAL LTD
Citation
PROTEOME SCIENCE, v.15
Abstract
Protein-protein interactions (PPIs) trigger a wide range of biological signaling pathways that are crucial for biomedical research and drug discovery. Various techniques have been used to study specific proteins, including affinity chromatography, activity-based probes, affinity-based probes and photo-affinity labeling (PAL). PAL has become one of the most powerful strategies to study PPIs. Traditional photocrosslinkers are used in PAL, including benzophenone, aryl azide, and diazirine. Upon photoirradiation, these photocrosslinkers (Pls) generate highly reactive species that react with adjacent molecules, resulting in a direct covalent modification. This review introduces recent examples of chemical proteomics study using PAL for PPIs.
Keywords
CARBOHYDRATE-BINDING PROTEIN; SITE-SPECIFIC INCORPORATION; UNNATURAL AMINO-ACIDS; CELL-CULTURE SILAC; CROSS-LINKING; PHOTOAFFINITY PROBES; LIVING CELLS; IN-VIVO; ESCHERICHIA-COLI; GENETIC-CODE; CARBOHYDRATE-BINDING PROTEIN; SITE-SPECIFIC INCORPORATION; UNNATURAL AMINO-ACIDS; CELL-CULTURE SILAC; CROSS-LINKING; PHOTOAFFINITY PROBES; LIVING CELLS; IN-VIVO; ESCHERICHIA-COLI; GENETIC-CODE; Photo-affinity probe; Protein-protein interaction; Quantitative proteomics; Benzophenone; Aryl azide; Diazirine
ISSN
1477-5956
URI
https://pubs.kist.re.kr/handle/201004/122614
DOI
10.1186/s12953-017-0123-3
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KIST Article > 2017
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