Journal
MOLECULES
Volume 18, Issue 9, Pages 10425-10451Publisher
MDPI
DOI: 10.3390/molecules180910425
Keywords
protein target identification; photoaffinity labeling; affinity chromatography; chemical proteomics; photo-crosslinking; bioorthogonal ligation; two step labeling; click chemistry
Funding
- KRCF Research Initiative Program
- National Research Foundation of Korea (NRF) [NRF-2012M3A9C4048774, NRF-2012M3A9C4048775, NRF-2012-0009543]
- Korean Ministry of Science, ICT and Future Planning
- National Research Foundation of Korea [2012M3A9C4048775, 2012-0009543] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Target identification of biologically active molecules such as natural products, synthetic small molecules, peptides, and oligonucleotides mainly relies on affinity chromatography, activity-based probes, or photoaffinity labeling (PAL). Amongst them, activity-based probes and PAL have offered great advantages in target identification technology due to their ability to form covalent bonds with the corresponding targets. Activity-based probe technology mainly relies on the chemical reactivity of the target proteins, thereby limiting the majority of the biological targets to enzymes or proteins which display reactive residues at the probe-binding site. In general, the probes should bear a reactive moiety such as an epoxide, a Michael acceptor, or a reactive alkyl halide in their structures. On the other hand, photoaffinity probes (PAPs) are composed of a target-specific ligand and a photoactivatable functional group. When bound to the corresponding target proteins and activated with wavelength-specific light, PAPs generate highly reactive chemical species that covalently cross-link proximal amino acid residues. This process is better known as PAL and is widely employed to identify cellular targets of biologically active molecules. This review highlights recent advances in target identification by PAL, with a focus on the structure and chemistry of the photoaffinity probes developed in the recent decade, coupled to the target proteins identified using these probes.
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