Dataset Information

Analysis of bilirubin-induced bovine serum albumin stability using protein denaturation and quantitative cross-linking mass spectrometry

ABSTRACT: We report the combination of protein-denaturation stability principles with quantitative cross-linking mass spectrometry using isobaric quantitative protein interaction reporter technologies. This method enables the evaluation of ligand-induced protein engagement through analysis of cross-link relative ratios across chemical denaturation. We found ligand-stabilized cross-linked lysine pairs in bovine serum albumin (BSA) and ligand bilirubin map to known binding sites Sudlow Site I and subdomain IB.

INSTRUMENT(S):

ORGANISM(S): Bos Taurus (bovine)

SUBMITTER: Martin Mathay

LAB HEAD: James E Bruce

PROVIDER: PXD036649 | Pride | 2024-07-03

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	210410_ureaXL_bsa_fwd_00M_rep1_1h_1.raw	Raw
	210410_ureaXL_bsa_fwd_00M_rep1_1h_2.raw	Raw
	210410_ureaXL_bsa_fwd_00M_rep1_1h_3.raw	Raw
	210410_ureaXL_bsa_fwd_02M_rep1_1h_1.raw	Raw
	210410_ureaXL_bsa_fwd_02M_rep1_1h_2.raw	Raw

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Publications

Studying Protein-Ligand Interactions by Protein Denaturation and Quantitative Cross-Linking Mass Spectrometry.

Mathay Martin M Keller Andrew A Bruce James E JE

Analytical chemistry 20230612 25

Recently, several mass spectrometry methods have utilized protein structural stability for the quantitative study of protein-ligand engagement. These protein-denaturation approaches, which include thermal proteome profiling (TPP) and stability of proteins from rates of oxidation (SPROX), evaluate ligand-induced denaturation susceptibility changes with a MS-based readout. The different techniques of bottom-up protein-denaturation methods each have their own advantages and challenges. Here, we rep ...[more]

PMID: 37307416

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