{"id":"5febede1-39b2-50c2-9f94-2a44f4d49c00","stable_key":"35ec55a7-323c-5c28-979e-3bdafe9d5769:yeast-diglucoside-null","predicate":"no_detected_change_in_recorded_experiment","statement":"Delphinidin 3,5-diglucoside showed no detected yeast alpha-glucosidase inhibition in the tested range.","claim_class":"observational","status":"source_derived_draft","evidence_grade":"ungraded","direction":"neutral","is_public":true,"mechanism_event_id":"8bd83c79-fe94-5722-b2e1-3f65e7d6e695","mechanism_event_label":"Delphinidin 3,5-diglucoside showed no detected yeast alpha-glucosidase inhibition in the tested range.","subject":{"id":"e6f59643-a0c4-5b62-8db1-1ae328c9b707","slug":"delphinidin-3-5-diglucoside","display_name":"Delphinidin 3,5-O-diglucoside / delphin","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":"8bd83c79-fe94-5722-b2e1-3f65e7d6e695","stable_key":"35ec55a7-323c-5c28-979e-3bdafe9d5769:yeast-diglucoside-null-event","event_type":"experimental_observation","label":"Delphinidin 3,5-diglucoside showed no detected yeast alpha-glucosidase inhibition in the tested range.","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":"e6f59643-a0c4-5b62-8db1-1ae328c9b707","slug":"delphinidin-3-5-diglucoside","display_name":"Delphinidin 3,5-O-diglucoside / delphin","entity_type_key":"small_molecule"},"role":"tested factor","stoichiometry":null,"state_label":"Delphinidin 3,5-diglucoside 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":"no_detected_change","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\": \"Delphinidin 3,5-diglucoside concentration series\", \"comparator\": \"No inhibitor\", \"endpoint\": \"Delphinidin 3,5-diglucoside showed no detected yeast alpha-glucosidase inhibition in the tested range.\", \"effect_direction\": \"no_detected_change\", \"combination\": \"single\", \"conditions\": []}","comparator":null,"unit":null,"notes":"Explicit extracted experimental comparison; source-derived draft.","entity":null},{"dimension":"experimental_model","value_text":"Yeast alpha-glucosidase synthetic-substrate assay.","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":"Assay-specific null; not every digestive enzyme or unlimited concentrations.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Delphinidin 3,5-diglucoside showed no detected yeast alpha-glucosidase inhibition in the tested range.","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":"2ae396b0-14b5-510c-a816-ee9b55a36ee1","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":"Yeast alpha-glucosidase synthetic-substrate assay.","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}