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Here, we compared the fluidity gradients of plasma membranes of the drug\u2010sensitive CHO cell line AuxB1 and its P\u2010glycoprotein overexpressing derivative B30 by fluorescence anisotropy of embedded\n                    <jats:italic>n<\/jats:italic>\n                    \u2010(9\u2010anthroyloxy) fatty acid probes (\n                    <jats:italic>n<\/jats:italic>\n                    \u2009=\u20092, 7, 9, 12, 16) in the temperature range of 10\u201350\u2009\u00b0C. The shape of the temperature profiles of probe mobility was comparable in AuxB1 and B30 membranes, but did not match. Overexpression of P\u2010glycoprotein smoothened the transversal gradient of the out\u2010of\u2010plane mode of rotation of the probes, which may facilitate the partitioning of hydrophobic drugs into the membrane and thereby increase the speed of P\u2010glycoprotein to pump the drug out of the cell.\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.70083","type":"journal-article","created":{"date-parts":[[2025,5,31]],"date-time":"2025-05-31T07:00:17Z","timestamp":1748674817000},"page":"2167-2178","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["P\u2010glycoprotein modulates the fluidity gradient of the plasma membrane of multidrug resistant\n                    <scp>CHO<\/scp>\n                    cells"],"prefix":"10.1002","volume":"599","author":[{"given":"Roger","family":"Busche","sequence":"first","affiliation":[{"name":"Institute for Biophysical Chemistry and Structural Biochemistry, 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