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Proteome-wide deconvolution of drug targets and binding sites by lysine reactivity profiling

ABSTRACT: This project describe a novel lysine reactivity profiling method for proteome-wide identification of drug targets and binding sites

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Mingliang Ye

PROVIDER: PXD031103 | JPOST Repository | Thu Jan 20 00:00:00 GMT 2022

REPOSITORIES: jPOST

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			Action	DRS
	HF_RCF20210821_DIALib_F1.raw	Raw
	HF_RCF20210821_DIALib_F2.raw	Raw
	HF_RCF20210821_DIALib_F3.raw	Raw
	HF_RCF20210821_DIALib_F4.raw	Raw
	HF_RCF20210821_DIALib_F5.raw	Raw

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Proteome-Wide Deconvolution of Drug Targets and Binding Sites by Lysine Reactivity Profiling

Project description:Recently, numerous efforts have been devoted to identifying drug targets and binding sites in complex proteomes, which is of great importance in modern drug discovery. In this study, we developed a robust lysine reactivity profiling method to systematically study drug-binding targets and binding sites at the proteome level. This method is based on the principle that binding of a drug to a specific region of target proteins will change the reactivity of lysine residues that are located at this region, and these changes can be detected with an enrichable and lysine reactive probe. Coupled with data-independent acquisition (DIA), the known target proteins and corresponding binding sites were successfully revealed from K562 cell lysates for three model drugs: geldanamycin, staurosporine, and dasatinib. In addition, the drug-induced conformational changes of certain targets were also revealed by our method during the screening of staurosporine. The screening sensitivity of our method revealed from the screening of stuarosporine and dasatinib was comparable with that of thermal proteome profiling (TPP) or machine learning-based limited proteolysis (LiP-Quant). Overall, 21 and 4 kinase targets, including adenosine 5′-triphosphate (ATP)-binding targets, were identified for staurosporine and dasatinib in K562 cell lysates, respectively. We found that target proteins identified by TPP, LiP-Quant, and our method were complementary, emphasizing that the development of new methods that probe different properties of proteins is of great importance in drug target deconvolution. We also envision further applications of our method in proteome-wide probing multiple events that involve lysine reactivity changes.

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