{"id":"c9fac45d-40c8-5ab7-9825-6deefe375958","stable_key":"d96b230c-481b-535b-930c-04eb87ec7f02:s-allylcysteine-iron-iii-binding","predicate":"binds_in_assay","statement":"Electrochemical measurements supported SAC binding of Fe3+; rat-brain assays also showed reduced iron-associated lipid peroxidation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"81b3babe-2e51-5741-b047-2ee32f8290b6","mechanism_event_label":"A second oxidation state was examined.","subject":{"id":"8c2c295d-68b3-5e62-b1a7-00fcf915e3cc","slug":"s-allylcysteine","display_name":"S-allyl-L-cysteine / SAC","entity_type_key":"small_molecule"},"object":{"id":"964be7ac-43bd-5f3e-8326-94f0590de67a","slug":"iron-iii","display_name":"Ferric iron","entity_type_key":"ion"},"evidence_count":1,"mechanism_event":{"id":"81b3babe-2e51-5741-b047-2ee32f8290b6","stable_key":"d96b230c-481b-535b-930c-04eb87ec7f02:s-allylcysteine-iron-iii-binding-event","event_type":"observed_relationship","label":"A second oxidation state was examined.","description":"Electrochemical measurements supported SAC binding of Fe3+; rat-brain assays also showed reduced iron-associated lipid peroxidation.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"8c2c295d-68b3-5e62-b1a7-00fcf915e3cc","slug":"s-allylcysteine","display_name":"S-allyl-L-cysteine / SAC","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"964be7ac-43bd-5f3e-8326-94f0590de67a","slug":"iron-iii","display_name":"Ferric iron","entity_type_key":"ion"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"acting_entity","value_text":"s-allylcysteine","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"dose","value_text":"Not specified in accessed abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"duration","value_text":"Not specified in accessed abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_comparison","value_text":"SAC in metal-binding and oxidative challenge assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Ferrozine, electrochemistry and rat brain homogenate","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"interpretation_status","value_text":"Source-derived research curation; not independent primary verification","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Does not establish iron depletion, removal from human tissues or treatment of iron overload.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"s-allylcysteine","display_name":"S-allyl-L-cysteine / SAC","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Cell-free assays and rat brain preparation","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"A second oxidation state was examined.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[18422331] Antioxidant and iron-binding properties of curcumin, capsaicin, and S-allylcysteine reduce oxidative stress in rat brain homogenate. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18422331/ · DOI 10.1021/jf0734931","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"route","value_text":"In vitro","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Ferrozine, electrochemistry and rat brain homogenate","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"f16839c7-1652-574c-9bd7-fa2624dc6032","evidence_kind":"source_excerpt","locator":"Lines 122-129","start_line":122,"end_line":129,"excerpt":"## s-allylcysteine-iron-iii-binding\nA second oxidation state was examined.\nElectrochemical measurements supported SAC binding of Fe3+; rat-brain assays also showed reduced iron-associated lipid peroxidation.\nModel: Ferrozine, electrochemistry and rat brain homogenate\nLimitations: Does not establish iron depletion, removal from human tissues or treatment of iron overload.\nEvidence access: Primary abstract\n[18422331] Antioxidant and iron-binding properties of curcumin, capsaicin, and S-allylcysteine reduce oxidative stress in rat brain homogenate. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18422331/ · DOI 10.1021/jf0734931\nStructured context: {\"organism\": \"Cell-free assays and rat brain preparation\", \"tissue_or_cell_type\": \"Ferrozine, electrochemistry and rat brain homogenate\", \"dose\": \"Not specified in accessed abstract\", \"duration\": \"Not specified in accessed abstract\", \"route\": \"In vitro\", \"experimental_comparison\": \"SAC in metal-binding and oxidative challenge assays\", \"acting_entity\": \"s-allylcysteine\", \"interpretation_status\": \"Source-derived research curation; not independent primary verification\"}","model_system":"Ferrozine, electrochemistry and rat brain homogenate","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; 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