ArticleProtein science : a publication of the Protein Society2022
Structure-based alteration of tryptophan residues of the multidrug transporter CmABCB1 to assess substrate binding using fluorescence spectroscopy.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 2 citations in OpenAlex.
- Structure-ATPase Activity Relationship of Rhodamine Derivatives as Potent Inhibitors of P-Glycoprotein CmABCB1.ACS medicinal chemistry letters · 2024Article
- Structure-based alteration of tryptophan residues of the multidrug transporter CmABCB1 to assess substrate binding using fluorescence spectroscopy.Protein science : a publication of the Protein Society · 2022Article
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7 authors at 1 institution in 1 country.
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Abstract
ABCB1, also known as P-glycoprotein, is an essential component of many physiological barriers and extrudes a variety of hydrophobic chemicals out of the cell. Structures of ABCB1 provided insights into the structural changes that occur upon ATP binding and the characteristic architecture of the substrate binding site. Yet, the structure-function relationship between substrate binding and transporting still remains largely obscured because there is no robust method for accurately measuring substrate binding constants. The methods currently used cannot identify whether the bound substrates are located in the inner chamber of the molecule in the transmembrane region or not because of the low spatial resolution. Here, we report a system for measuring the affinity of substrate binding to the Cyanidioschyzon merolae ABCB1 (CmABCB1) using site-specific tryptophan (Trp) fluorescence quenching. We designed a CmABCB1 mutant with an extrinsic Trp residue introduced into the inner chamber. Trp fluorescence was quenched by three substrates and one inhibitor, including rhodamine 6G, in a saturable fashion, allowing for accurate estimation of the dissociation constant (K
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