Component

Mangiferin-ferric iron complex, assay-defined

Mangiferin-ferric iron complex, assay-defined. Species, exposure and limitations are retained in each linked claim.

3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. The ferric complex protected mitochondrial glutathione against oxidation.

    Mangiferin-ferric iron complex, assay-defined → Rat liver mitochondrial glutathione oxidation or depletion source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/mangiferin-research/17068204.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64", "start_char": 0, "end_char": 1172, "text_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64"}
    experimental_model
    Iron-coordination spectroscopy and mitochondrial challenge
    exposure
    Assay-defined ferric iron-mangiferin complex
    limitations
    Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation.
    nutrient_topic
    Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
    organism
    Rattus norvegicus and cell-free chemistry
    plain_language
    Metal coordination altered protection of the redox buffer.
    primary_references
    [mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. (2007). https://pubmed.ncbi.nlm.nih.gov/17068204/ DOI: 10.1124/jpet.106.112003
    tissue_or_cell_type
    Isolated mitochondria

    Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 757–768

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Iron-coordination spectroscopy and mitochondrial challenge · source_derived_draft · unverified_draft

    ### mangiferin-complex-gsh The ferric complex protected mitochondrial glutathione against oxidation. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Metal coordination altered protection of the redox buffer. organism: Rattus norvegicus and cell-free chemistry tissue_or_cell_type: Isolated mitochondria experimental_model: Iron-coordination spectroscopy and mitochondrial challenge limitations: Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation. exposure: Assay-defined ferric iron-mangiferin complex evidence_span: {"source_cache": "artifacts/mangiferin-research/17068204.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64", "start_char": 0, "end_char": 1172, "text_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64"} [mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. (2007). https://pubmed.ncbi.nlm.nih.gov/17068204/ DOI: 10.1124/jpet.106.112003
    Complete structured claim and evidence

  2. The ferric complex did not elicit permeability transition and protected against its induction in the assay.

    Mangiferin-ferric iron complex, assay-defined → Rat liver mitochondrial permeability transition source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/mangiferin-research/17068204.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64", "start_char": 0, "end_char": 1172, "text_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64"}
    experimental_model
    Iron-coordination spectroscopy and mitochondrial challenge
    exposure
    Assay-defined ferric iron-mangiferin complex
    limitations
    Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation.
    nutrient_topic
    Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
    organism
    Rattus norvegicus and cell-free chemistry
    plain_language
    Changing chemical form changed the membrane response.
    primary_references
    [mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. (2007). https://pubmed.ncbi.nlm.nih.gov/17068204/ DOI: 10.1124/jpet.106.112003
    tissue_or_cell_type
    Isolated mitochondria

    Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 744–755

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Iron-coordination spectroscopy and mitochondrial challenge · source_derived_draft · unverified_draft

    ### mangiferin-complex-mpt The ferric complex did not elicit permeability transition and protected against its induction in the assay. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Changing chemical form changed the membrane response. organism: Rattus norvegicus and cell-free chemistry tissue_or_cell_type: Isolated mitochondria experimental_model: Iron-coordination spectroscopy and mitochondrial challenge limitations: Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation. exposure: Assay-defined ferric iron-mangiferin complex evidence_span: {"source_cache": "artifacts/mangiferin-research/17068204.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64", "start_char": 0, "end_char": 1172, "text_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64"} [mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. (2007). https://pubmed.ncbi.nlm.nih.gov/17068204/ DOI: 10.1124/jpet.106.112003
    Complete structured claim and evidence

What acts on it

  1. Electrochemical and spectroscopic analyses supported coordination of ferric iron with mangiferin.

    Mangiferin → Mangiferin-ferric iron complex, assay-defined source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/mangiferin-research/17068204.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64", "start_char": 0, "end_char": 1172, "text_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64"}
    experimental_model
    Iron-coordination spectroscopy and mitochondrial challenge
    exposure
    Assay-defined ferric iron-mangiferin complex
    limitations
    Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation.
    nutrient_topic
    Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
    organism
    Rattus norvegicus and cell-free chemistry
    plain_language
    The metal-bound form is represented separately.
    primary_references
    [mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. (2007). https://pubmed.ncbi.nlm.nih.gov/17068204/ DOI: 10.1124/jpet.106.112003
    tissue_or_cell_type
    Isolated mitochondria

    Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 731–742

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Iron-coordination spectroscopy and mitochondrial challenge · source_derived_draft · unverified_draft

    ### mangiferin-ferric-complex Electrochemical and spectroscopic analyses supported coordination of ferric iron with mangiferin. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The metal-bound form is represented separately. organism: Rattus norvegicus and cell-free chemistry tissue_or_cell_type: Isolated mitochondria experimental_model: Iron-coordination spectroscopy and mitochondrial challenge limitations: Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation. exposure: Assay-defined ferric iron-mangiferin complex evidence_span: {"source_cache": "artifacts/mangiferin-research/17068204.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64", "start_char": 0, "end_char": 1172, "text_sha256": "1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64"} [mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. (2007). https://pubmed.ncbi.nlm.nih.gov/17068204/ DOI: 10.1124/jpet.106.112003
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards