{"id":"372fabff-814e-52d0-990a-07cd54cdd1a6","stable_key":"35ec55a7-323c-5c28-979e-3bdafe9d5769:yeast-glucosidase-delphinidin-3-glucoside","predicate":"decreases_in_recorded_experiment","statement":"delphinidin-3-glucoside inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 364 uM.","claim_class":"observational","status":"source_derived_draft","evidence_grade":"ungraded","direction":"negative","is_public":true,"mechanism_event_id":"b8593020-323c-5c2b-bbbc-cad1e5441635","mechanism_event_label":"delphinidin-3-glucoside inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 364 uM.","subject":{"id":"5a3646a9-d8c9-5925-b6a8-beebe930333c","slug":"delphinidin-3-glucoside","display_name":"Delphinidin 3-O-beta-D-glucopyranoside","entity_type_key":"small_molecule"},"object":{"id":"5a14cf90-37db-59d9-918f-0effcb510f9d","slug":"yeast-alpha-glucosidase","display_name":"Saccharomyces cerevisiae alpha-glucosidase assay enzyme","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"b8593020-323c-5c2b-bbbc-cad1e5441635","stable_key":"35ec55a7-323c-5c28-979e-3bdafe9d5769:yeast-glucosidase-delphinidin-3-glucoside-event","event_type":"experimental_observation","label":"delphinidin-3-glucoside inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 364 uM.","description":"**Enzyme identity changes the digestive-enzyme claim.** A purified-compound assay used yeast α-glucosidase and a synthetic substrate, not human sucrase-isomaltase. Delphinidin aglycone inhibited with an IC50 near 4.11 µM; cyanidin was about 17.01 µM. Delphinidin-3-glucoside was much weaker, around 364 µM, and its 3,5-diglucoside showed no detected inhibition in the tested range. These values establish structure-dependent assay behavior. They cannot be imported as human intestinal IC50 values or a clinical comparison with acarbose. Docking does not repair that species/substrate gap. [Promyos et al., 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/).","status":"provisional","compartment":null,"participants":[{"entity":{"id":"5a3646a9-d8c9-5925-b6a8-beebe930333c","slug":"delphinidin-3-glucoside","display_name":"Delphinidin 3-O-beta-D-glucopyranoside","entity_type_key":"small_molecule"},"role":"tested factor","stoichiometry":null,"state_label":"Purified delphinidin-3-glucoside concentration series","sequence_order":0,"notes":""},{"entity":{"id":"5a14cf90-37db-59d9-918f-0effcb510f9d","slug":"yeast-alpha-glucosidase","display_name":"Saccharomyces cerevisiae alpha-glucosidase assay enzyme","entity_type_key":"protein"},"role":"measured outcome","stoichiometry":null,"state_label":"decrease","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Full text retrieved; relevant methods/results/figure text reviewed. No independent raw-data verification.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_contrast","value_text":"{\"intervention\": \"Purified delphinidin-3-glucoside concentration series\", \"comparator\": \"Assay without inhibitor\", \"endpoint\": \"delphinidin-3-glucoside inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 364 uM.\", \"effect_direction\": \"decrease\", \"combination\": \"single\", \"conditions\": []}","comparator":null,"unit":null,"notes":"Explicit extracted experimental comparison; source-derived draft.","entity":null},{"dimension":"experimental_model","value_text":"Saccharomyces cerevisiae alpha-glucosidase, pNPG substrate, pH 6, 37 C.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"interpretation_status","value_text":"Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Yeast enzyme assay; not human sucrase-isomaltase or maltase. IC50 depends on substrate and conditions; docking is not a human-target validation.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"delphinidin-3-glucoside inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 364 uM.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Investigation of Anthocyanidins and Anthocyanins for Targeting α-Glucosidase in Diabetes Mellitus. | 2020 | DOI 10.3746/pnf.2020.25.3.263 | PMID 33083375 | https://pubmed.ncbi.nlm.nih.gov/33083375/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/ | https://doi.org/10.3746/pnf.2020.25.3.263","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"source_locator","value_text":"Reviewed reference lines 80-80; exact primary location described in quoted passage where extracted.","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"8f844236-009a-563d-a6b1-20bdbcb54e59","evidence_kind":"source_excerpt","locator":"Lines 80-80","start_line":80,"end_line":80,"excerpt":"**Enzyme identity changes the digestive-enzyme claim.** A purified-compound assay used yeast α-glucosidase and a synthetic substrate, not human sucrase-isomaltase. Delphinidin aglycone inhibited with an IC50 near 4.11 µM; cyanidin was about 17.01 µM. Delphinidin-3-glucoside was much weaker, around 364 µM, and its 3,5-diglucoside showed no detected inhibition in the tested range. These values establish structure-dependent assay behavior. They cannot be imported as human intestinal IC50 values or a clinical comparison with acarbose. Docking does not repair that species/substrate gap. [Promyos et al., 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/).","model_system":"Saccharomyces cerevisiae alpha-glucosidase, pNPG substrate, pH 6, 37 C.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Exact excerpt of the retained AI-assisted reviewed reference; primary sources are cited in primary_references and access scope is retained. Not a verbatim quotation from a primary paper.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"b08e7f7d-4d34-56d7-a185-2124f8d72b3c","stable_key":"import-35ec55a7-323c-5c28-979e-3bdafe9d5769","title":"Anthocyanins: detailed mechanisms of action (reviewed 4 October 2026)","document_type":"imported_text","citation_label":"Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication.","file_path":"","sha256":"7cff1a47fbd9c625412b84162b1c823004b4162b7c009f9a11d5807fb8e04ef9","revision_id":"1bd4fa42-bfeb-5148-8250-fc363d8c1de0","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}