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Compounds\n                    <jats:bold>1<\/jats:bold>\n                    and\n                    <jats:bold>2<\/jats:bold>\n                    represent the first examples of this skeletal type from the genus\n                    <jats:italic>Viburnum<\/jats:italic>\n                    . The structures of the new compounds were elucidated by comprehensive analysis of their 1D and 2D NMR, HRESIMS, and ECD data. All isolates were evaluated for their inhibitory activities against\n                    <jats:italic>\u03b1<\/jats:italic>\n                    \u2010amylase and\n                    <jats:italic>\u03b1<\/jats:italic>\n                    \u2010glucosidase, key enzymes involved in carbohydrate metabolism. Among them, compound\n                    <jats:bold>1<\/jats:bold>\n                    exhibited inhibitory activities against\n                    <jats:italic>\u03b1<\/jats:italic>\n                    \u2010amylase (IC\n                    <jats:sub>50<\/jats:sub>\n                    = 38.20 \u00b5M) and\n                    <jats:italic>\u03b1<\/jats:italic>\n                    \u2010glucosidase (IC\n                    <jats:sub>50<\/jats:sub>\n                    = 24.15 \u00b5M), comparable to those of acarbose (IC\n                    <jats:sub>50<\/jats:sub>\n                    = 39.19 and 25.73 \u00b5M, respectively). Molecular docking studies suggested that compound\n                    <jats:bold>1<\/jats:bold>\n                    bound to the active sites of both enzymes via hydrogen bonding and hydrophobic interactions.\n                  <\/jats:p>","DOI":"10.1002\/cbdv.71650","type":"journal-article","created":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T18:19:45Z","timestamp":1788200385000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Constituents From the Flowers of\n                    <i>Viburnum macrocephalum<\/i>\n                    f.\n                    <i>macrocephalum<\/i>\n                    and Their\n                    <i>\u03b1<\/i>\n                    \u2010Amylase and\n                    <i>\u03b1<\/i>\n                    \u2010Glucosidase Inhibitory Activities"],"prefix":"10.1002","volume":"23","author":[{"given":"Ya\u2010Jiao","family":"Chen","sequence":"first","affiliation":[{"name":"College of Bioscience and Biotechnology Yangzhou University  Yangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong\u2010Juan","family":"Zhou","sequence":"additional","affiliation":[{"name":"College of Bioscience and Biotechnology Yangzhou University  Yangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xue\u2010Jing","family":"Zhu","sequence":"additional","affiliation":[{"name":"College of Bioscience and Biotechnology Yangzhou University  Yangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jia","family":"Chen","sequence":"additional","affiliation":[{"name":"College of Bioscience and Biotechnology Yangzhou University  Yangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jian\u2010Hua","family":"Shao","sequence":"additional","affiliation":[{"name":"College of Bioscience and Biotechnology Yangzhou University  Yangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7941-8175","authenticated-orcid":false,"given":"Chun\u2010Chao","family":"Zhao","sequence":"additional","affiliation":[{"name":"College of Bioscience and Biotechnology Yangzhou University  Yangzhou China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,8,31]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1111\/jse.12526"},{"key":"e_1_2_9_3_1","unstructured":"H. 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