{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,26]],"date-time":"2025-10-26T21:40:51Z","timestamp":1761514851675,"version":"build-2065373602"},"reference-count":32,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2022,1,23]],"date-time":"2022-01-23T00:00:00Z","timestamp":1642896000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81873193","21904022","82173952"],"award-info":[{"award-number":["81873193","21904022","82173952"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Rapid Comm Mass Spectrometry"],"published-print":{"date-parts":[[2022,3,30]]},"abstract":"<jats:sec>\n                    <jats:title>Rationale<\/jats:title>\n                    <jats:p>A large number of studies have shown that the production of aberrant and deleterious copper zinc superoxide dismutase (SOD1) species is closely related to amyotrophic lateral sclerosis (ALS). Therefore, it is of great significance to screen effective inhibitors of misfolding and aggregation of SOD1 for treating ALS disease.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>The interaction between flavanone compounds with apo\u2010SOD1was investigated using native electrospray ion mobility mass spectrometry (native ESI\u2010IM\u2010MS). Binding affinities of ligands were compared using native MS, ESI\u2010MS\/MS, collision\u2010induced unfolding, and competitive experiments. The effect of ligands on apo\u2010SOD1 aggregation was investigated using the fluorescence spectroscopy method.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>The results of MS showed that the binding affinity of liquiritin apioside was the strongest, better than the corresponding monosaccharide and aglycone, indicating that the presence and the number of glycosyl group are beneficial to enhance ligand affinity to protein. The results of fluorescence spectroscopy for inhibiting protein aggregation in vitro were consistent with the binding affinity. In addition, the results of the collision\u2010induced unfolding indicated that liquiritin apioside can slow down the unfolding of the protein. Meanwhile, the results of competition experiment suggested that liquiritin apiosides share different binding sites with naringin and 5\u2010fluorouridine, which are significant for the structural stability of SOD1.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>This study revealed that the binding of liquiritin apioside can stabilize apo\u2010SOD1 dimer and inhibit the aggregation of apo\u2010SOD1, and illustrated that native ESI\u2010IM\u2010MS is a powerful tool for providing insight into investigating the structure\u2013activity relationship between small molecules and protein, and screening protein conformation stabilizers.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1002\/rcm.9251","type":"journal-article","created":{"date-parts":[[2022,1,2]],"date-time":"2022-01-02T23:35:58Z","timestamp":1641166558000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Screening apo\u2010SOD1 conformation stabilizers from natural flavanones using native ion mobility mass spectrometry and fluorescence spectroscopy methods"],"prefix":"10.1002","volume":"36","author":[{"given":"Bing","family":"Zhao","sequence":"first","affiliation":[{"name":"State Key Laboratory of Crop Stress Adaptation and Improvement, Henan Joint International Laboratory for Crop Muti\u2010Omics Research, School of Life Sciences Henan University  Kaifeng China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xinyu","family":"Bian","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Electroanalytical Chemistry, National Center of Mass Spectrometry in Changchun, Jilin 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