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The structure\u2010activity study revealed that both the iminosugar and the light\u2010sensitive azobenzene are essential features to exert inhibitory activity towards human GCase and a system with the correct inhibition trend (IC\n                    <jats:sub>50<\/jats:sub>\n                    of the light\u2010activated form lower than IC\n                    <jats:sub>50<\/jats:sub>\n                    of the dark form) was identified. Kinetic analyses showed that all compounds are non\u2010competitive inhibitors (mixed or pure) of GCase and the enzyme allosteric site involved in the interaction was identified by means of MD simulations. A moderate activity enhancement of mutant GCase assessed in GD patients' fibroblasts (ex vivo experiments) carrying the most common mutation was recorded. This promising observation paves the way for further studies to improve the benefit of the light\u2010to\u2010dark thermal conversion for chaperoning activity.\n                  <\/jats:p>","DOI":"10.1002\/chem.202203841","type":"journal-article","created":{"date-parts":[[2023,1,4]],"date-time":"2023-01-04T08:00:20Z","timestamp":1672819220000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Light\u2010Triggered Control of Glucocerebrosidase Inhibitors: Towards Photoswitchable Pharmacological Chaperones"],"prefix":"10.1002","volume":"29","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9899-0836","authenticated-orcid":false,"given":"Francesca","family":"Clemente","sequence":"first","affiliation":[{"name":"Department of Chemistry \u201cU. 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