Component

Human serum albumin

Human circulating albumin; PLP-binding protein.

10 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. Equilibrium dialysis found one higher-affinity human-albumin PLP-binding site (Kd 8.7 micromolar) and additional lower-affinity sites.

    Human serum albumin → PLP source_derived_draftungraded
    Experimental context and source evidence
    evidence_location
    Indexed abstract: equilibrium dialysis and competition
    experimental_model
    Purified human serum albumin binding assays.
    exposure
    In-vitro albumin/PLP binding.
    limitations
    Purified-system affinity is not a plasma sufficiency threshold; bovine albumin behaved differently.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Homo sapiens
    plain_language
    Albumin binds circulating active B6.
    primary_references
    [fonda1991] The binding of pyridoxal 5'-phosphate to human serum albumin. (1991). https://pubmed.ncbi.nlm.nih.gov/1898027/ DOI: 10.1016/0003-9861(91)90167-h
    tissue_or_cell_type
    Purified serum albumin

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 335–346

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human serum albumin binding assays. · source_derived_draft · unverified_draft

    ### b6-transport-albumin-binding Equilibrium dialysis found one higher-affinity human-albumin PLP-binding site (Kd 8.7 micromolar) and additional lower-affinity sites. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Albumin binds circulating active B6. organism: Homo sapiens tissue_or_cell_type: Purified serum albumin experimental_model: Purified human serum albumin binding assays. limitations: Purified-system affinity is not a plasma sufficiency threshold; bovine albumin behaved differently. exposure: In-vitro albumin/PLP binding. evidence_location: Indexed abstract: equilibrium dialysis and competition [fonda1991] The binding of pyridoxal 5'-phosphate to human serum albumin. (1991). https://pubmed.ncbi.nlm.nih.gov/1898027/ DOI: 10.1016/0003-9861(91)90167-h
    Complete structured claim and evidence

  2. Albumin reduced palmitoylcarnitine-associated oxidative stress and membrane-potential impairment in donor leukocytes.

    Human serum albumin → Human leukocyte oxidative stress during palmitoylcarnitine exposure source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and full-text PBMC exposure methods and results
    experimental_model
    Human PBMCs with 5 mg/ml human serum albumin, given 30 minutes before or alongside the four-hour exposure.
    limitations
    This comparison does not by itself prove a binding mechanism or clinical efficacy.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The surrounding protein environment changed the observed effect.
    primary_references
    Palmitoylcarnitine impairs immunity in decompensated cirrhosis. · 2024 · https://pubmed.ncbi.nlm.nih.gov/39524205/ · DOI 10.1016/j.jhepr.2024.101187

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 522–528

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human PBMCs with 5 mg/ml human serum albumin, given 30 minutes before or alongside the four-hour exposure. · source_derived_draft · unverified_draft

    ## l-carnitine-acyl-albumin The surrounding protein environment changed the observed effect. Albumin reduced palmitoylcarnitine-associated oxidative stress and membrane-potential impairment in donor leukocytes. Model: Human PBMCs with 5 mg/ml human serum albumin, given 30 minutes before or alongside the four-hour exposure. Limitations: This comparison does not by itself prove a binding mechanism or clinical efficacy. Evidence access: Primary abstract and full-text PBMC exposure methods and results Palmitoylcarnitine impairs immunity in decompensated cirrhosis. · 2024 · https://pubmed.ncbi.nlm.nih.gov/39524205/ · DOI 10.1016/j.jhepr.2024.101187
    Complete structured claim and evidence

What acts on it

  1. Luteolin sulfate formed a more stable albumin complex than parent luteolin.

    Luteolin 3′-O-sulfate → Human serum albumin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human serum-albumin binding assay.
    limitations
    Binding alone does not establish displacement toxicity.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    Conjugation changes carrier binding.
    primary_references
    Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36481402/ · DOI 10.1016/j.biopha.2022.114078

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 236–242

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human serum-albumin binding assay. · source_derived_draft · unverified_draft

    ## luteolin-albumin-sulfate Conjugation changes carrier binding. Luteolin sulfate formed a more stable albumin complex than parent luteolin. Model: Human serum-albumin binding assay. Limitations: Binding alone does not establish displacement toxicity. Evidence access: Primary abstract Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36481402/ · DOI 10.1016/j.biopha.2022.114078
    Complete structured claim and evidence

  2. The parent bound human serum albumin with high affinity and moderately displaced the Site I marker warfarin in vitro.

    Myricetin → Human serum albumin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Albumin fluorescence and ultrafiltration assays.
    limitations
    Not demonstrated displacement toxicity or a change in patient anticoagulation.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    Carrier binding changes the freely available fraction.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 124–130

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Albumin fluorescence and ultrafiltration assays. · source_derived_draft · unverified_draft

    ## myricetin-parent-albumin Carrier binding changes the freely available fraction. The parent bound human serum albumin with high affinity and moderately displaced the Site I marker warfarin in vitro. Model: Albumin fluorescence and ultrafiltration assays. Limitations: Not demonstrated displacement toxicity or a change in patient anticoagulation. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    Complete structured claim and evidence

  3. The sulfate bound human serum albumin with high affinity and moderately displaced the Site I marker warfarin in vitro.

    Myricetin 3′-O-sulfate → Human serum albumin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Albumin fluorescence and ultrafiltration assays.
    limitations
    Not demonstrated displacement toxicity or a change in patient anticoagulation.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    Carrier binding changes the freely available fraction.
    primary_references
    Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 172–178

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Albumin fluorescence and ultrafiltration assays. · source_derived_draft · unverified_draft

    ## myricetin-sulfate-albumin Carrier binding changes the freely available fraction. The sulfate bound human serum albumin with high affinity and moderately displaced the Site I marker warfarin in vitro. Model: Albumin fluorescence and ultrafiltration assays. Limitations: Not demonstrated displacement toxicity or a change in patient anticoagulation. Evidence access: Primary full text Interaction of myricetin, ampelopsin (dihydromyricetin), and their sulfate metabolites with serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion-transporting polypeptides (OATP1B1 and OATP2B1). · 2024 · https://pubmed.ncbi.nlm.nih.gov/39344282/ · DOI 10.1002/prp2.70021
    Complete structured claim and evidence

  4. Naringenin sulfate conjugates formed more stable complexes with human serum albumin than the parent flavonoid in vitro.

    Naringenin sulfate conjugates → Human serum albumin source_derived_draftungraded
    Experimental context and source evidence
    dose
    Naringenin and sulfate/glucuronide conjugates
    duration
    Equilibrium assay
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    evidence_scope
    literature_reviewed; model-specific source-derived curation
    experimental_model
    Cell-free human serum albumin binding assays
    limitations
    Binding does not establish tissue delivery or a clinically important displacement interaction.
    nutrient_topic
    Naringenin chapter; interacting nutrients, drugs, peptides and proteins retain their experimental settings. · Naringenin
    organism
    Cell-free human serum albumin binding assays
    plain_language
    Naringenin sulfate conjugates formed more stable complexes with human serum albumin than the parent flavonoid in vitro.
    primary_references
    Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. (2023). https://pubmed.ncbi.nlm.nih.gov/36481402/ DOI: 10.1016/j.biopha.2022.114078
    route
    In vitro
    tissue
    Ligand-protein binding

    Naringenin: mechanism of action and interactions (2026-09-20) · lines 66–75

    Original AI-assisted source-specific curation with primary-study citations, model, exposure, route, duration, negative findings and limitations preserved. Not publisher full text. · supports · Cell-free human serum albumin binding assays · source_derived_draft · unverified_draft

    ## naringenin-conjugate-albumin Naringenin sulfate conjugates formed more stable complexes with human serum albumin than the parent flavonoid in vitro. Model/species: Cell-free human serum albumin binding assays Tissue/system: Ligand-protein binding Exposure: Naringenin and sulfate/glucuronide conjugates Route: In vitro Duration: Equilibrium assay Limits: Binding does not establish tissue delivery or a clinically important displacement interaction. Primary reference: Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. (2023). https://pubmed.ncbi.nlm.nih.gov/36481402/ DOI: 10.1016/j.biopha.2022.114078 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence

  5. Human albumin bound NO2-CLA noncovalently and formed covalent adducts at Cys34.

    Nitro-conjugated linoleic acid / NO2-CLA family → Human serum albumin source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified protein and chemical assays.
    limitations
    Distribution was a mechanistic implication, not a measured clinical outcome.
    nutrient_topic
    CLA collection; isomer, preparation, species, exposure and manipulation remain explicit. · Conjugated linoleic acid / CLA isomer family
    plain_language
    A circulating carrier can bind the modified lipid in two ways.
    primary_references
    The Chemical Basis of Thiol Addition to Nitro-conjugated Linoleic Acid, a Protective Cell-signaling Lipid. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27923813/ · DOI 10.1074/jbc.M116.756288

    Conjugated linoleic acid: isomers, signaling, nutrient interactions and discovery (2026-09-19) · lines 350–356

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified protein and chemical assays. · source_derived_draft · unverified_draft

    ## cla-albumin A circulating carrier can bind the modified lipid in two ways. Human albumin bound NO2-CLA noncovalently and formed covalent adducts at Cys34. Model: Purified protein and chemical assays. Limitations: Distribution was a mechanistic implication, not a measured clinical outcome. Evidence access: Primary abstract The Chemical Basis of Thiol Addition to Nitro-conjugated Linoleic Acid, a Protective Cell-signaling Lipid. · 2017 · https://pubmed.ncbi.nlm.nih.gov/27923813/ · DOI 10.1074/jbc.M116.756288
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Pyridoxal and 4-pyridoxic acid inhibited PLP binding to human serum albumin in vitro.

    Pyridoxal → PLP source_derived_draftungraded
    Experimental context and source evidence
    evidence_location
    Indexed abstract: equilibrium dialysis and competition
    experimental_model
    Purified human serum albumin binding assays.
    exposure
    In-vitro binding-inhibition experiments.
    limitations
    Physiological competition magnitude and consequences were not established.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Homo sapiens
    plain_language
    Related B6 molecules can compete in albumin-binding assays.
    primary_references
    [fonda1991] The binding of pyridoxal 5'-phosphate to human serum albumin. (1991). https://pubmed.ncbi.nlm.nih.gov/1898027/ DOI: 10.1016/0003-9861(91)90167-h
    tissue_or_cell_type
    Purified serum albumin

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 348–359

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human serum albumin binding assays. · source_derived_draft · unverified_draft

    ### b6-transport-albumin-competition Pyridoxal and 4-pyridoxic acid inhibited PLP binding to human serum albumin in vitro. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Related B6 molecules can compete in albumin-binding assays. organism: Homo sapiens tissue_or_cell_type: Purified serum albumin experimental_model: Purified human serum albumin binding assays. limitations: Physiological competition magnitude and consequences were not established. exposure: In-vitro binding-inhibition experiments. evidence_location: Indexed abstract: equilibrium dialysis and competition [fonda1991] The binding of pyridoxal 5'-phosphate to human serum albumin. (1991). https://pubmed.ncbi.nlm.nih.gov/1898027/ DOI: 10.1016/0003-9861(91)90167-h
    Complete structured claim and evidence

  2. V(V) and V(IV) bound vacant transferrin iron-binding sites in culture medium even with a 20-fold molar excess of albumin, without displacing already-bound Fe(III) under those conditions.

    Vanadate(V), protonation/speciation dependent → Human serum transferrin / TF source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human transferrin binding experiments under normoxic conditions.
    limitations
    Does not establish systemic iron deficiency or competition magnitude at dietary exposures.
    nutrient_topic
    Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
    plain_language
    Vanadium can occupy available metal-binding sites without stripping out all bound iron.
    primary_references
    Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926

    Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 190–196

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transferrin binding experiments under normoxic conditions. · source_derived_draft · unverified_draft

    ## vanadium-tf-binding Vanadium can occupy available metal-binding sites without stripping out all bound iron. V(V) and V(IV) bound vacant transferrin iron-binding sites in culture medium even with a 20-fold molar excess of albumin, without displacing already-bound Fe(III) under those conditions. Model: Human transferrin binding experiments under normoxic conditions. Limitations: Does not establish systemic iron deficiency or competition magnitude at dietary exposures. Evidence access: Primary abstract Vanadium(V/IV)-Transferrin Binding Disrupts the Transferrin Cycle and Reduces Vanadium Uptake and Antiproliferative Activity in Human Lung Cancer Cells. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32578416/ · DOI 10.1021/acs.inorgchem.0c00926
    Complete structured claim and evidence

  3. Plasma zinc correlated with plasma albumin in the cirrhosis and malabsorption groups, supporting albumin as one contributor to lower measured circulating zinc.

    Plasma albumin concentration → Plasma zinc concentration source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    cross_nutrient
    Human serum albumin (carrier_protein)
    evidence_location
    Indexed primary abstract.
    evidence_span
    {"source_cache": "artifacts/zinc-clinical-sources/walker1973.abstract.txt", "locator": "Primary indexed abstract; complete local file", "file_sha256": "350425d75c9023c5b9ddb97d734e320b4e07c6fe5b834213defb1adc7cc26b00", "utf8_bytes": 991}
    experimental_model
    Observational comparison of 19 malabsorption patients, 21 cirrhosis patients, 20 controls and 23 other disease patients
    exposure
    Fasting and post-meal plasma samples; disease-group comparisons.
    limitations
    Correlations cannot distinguish dietary shortage from albumin binding, redistribution and disease effects. Plasma measurements are not intracellular zinc thresholds.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    A lower carrier-protein level can help explain a lower plasma zinc reading.
    primary_references
    [zn-clin-walker1973] Plasma and urinary zinc in patients with malabsorption syndromes or hepatic cirrhosis. (1973). https://pubmed.ncbi.nlm.nih.gov/4785284/ DOI: 10.1136/gut.14.12.943
    tissue_or_cell_type
    Plasma and urine
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 1452–1465

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Observational comparison of 19 malabsorption patients, 21 cirrhosis patients, 20 controls and 23 other disease patients · source_derived_draft · unverified_draft

    ### zn-clin-plasma-albumin Plasma zinc correlated with plasma albumin in the cirrhosis and malabsorption groups, supporting albumin as one contributor to lower measured circulating zinc. Condition category: biomarker_context nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: A lower carrier-protein level can help explain a lower plasma zinc reading. organism: Homo sapiens tissue_or_cell_type: Plasma and urine experimental_model: Observational comparison of 19 malabsorption patients, 21 cirrhosis patients, 20 controls and 23 other disease patients limitations: Correlations cannot distinguish dietary shortage from albumin binding, redistribution and disease effects. Plasma measurements are not intracellular zinc thresholds. exposure: Fasting and post-meal plasma samples; disease-group comparisons. cross_nutrient: Human serum albumin (carrier_protein) evidence_location: Indexed primary abstract. evidence_span: {"source_cache": "artifacts/zinc-clinical-sources/walker1973.abstract.txt", "locator": "Primary indexed abstract; complete local file", "file_sha256": "350425d75c9023c5b9ddb97d734e320b4e07c6fe5b834213defb1adc7cc26b00", "utf8_bytes": 991} [zn-clin-walker1973] Plasma and urinary zinc in patients with malabsorption syndromes or hepatic cirrhosis. (1973). https://pubmed.ncbi.nlm.nih.gov/4785284/ DOI: 10.1136/gut.14.12.943
    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