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A peptide-centric local stability assay enables proteome-scale identification of the protein targets of diverse ligands

ABSTRACT: We found that ligand-induced protein local stability shifts can be sensitively detected on a proteome-wide scale by a limited proteolysis strategy using a large amount of trypsin to generate and analyze peptides directly from native proteins. This enabled the development of the “peptide-centric local stability assay” (PELSA), a modification-free approach that achieves unprecedented sensitivity in proteome-wide target identification and binding-region determination. We demonstrate the versatility of PELSA by investigating the interactions across various biological contexts.

INSTRUMENT(S): Orbitrap Exploris 480, Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): T Cell, Leukocyte, Epithelial Cell, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: KEJIA LI

LAB HEAD: Mingliang Ye

PROVIDER: PXD034606 | Pride | 2024-11-26

REPOSITORIES: pride

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			Action	DRS
	20230507_OE480_FAIMS_LKJ1_Cap_HeLa_PELSA_10E_Control_1.raw	Raw
	20230507_OE480_FAIMS_LKJ1_Cap_HeLa_PELSA_10E_Control_2.raw	Raw
	20230507_OE480_FAIMS_LKJ1_Cap_HeLa_PELSA_10E_Control_3.raw	Raw
	20230507_OE480_FAIMS_LKJ1_Cap_HeLa_PELSA_10E_Control_4.raw	Raw
	20230507_OE480_FAIMS_LKJ1_Cap_HeLa_PELSA_2E_Control_1.raw	Raw

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