Component

Cucurbitacin E

Context-specific entity; species, compartment and exposure are stated on each claim.

6 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. Incubating purified human cofilin 1 with cucurbitacin E produced covalent adducts; mass shifts were compatible with about four compound molecules per cofilin under the tested excess-compound conditions.

    Cucurbitacin E → Human cofilin 1 / CFL1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC3751690
    experimental_model
    Purified human cofilin 1, 5 micromolar; up to 1:100 protein:compound molar ratio, 16 hours.
    limitations
    Long, high-excess biochemical incubation; does not establish selectivity or occupancy after human ingestion.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Protein cysteines can become chemical attachment sites.
    primary_references
    Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23945128/ · DOI 10.1186/1478-811X-11-58

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 20–26

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human cofilin 1, 5 micromolar; up to 1:100 protein:compound molar ratio, 16 hours. · source_derived_draft · unverified_draft

    ## cucurbitacin-e-cofilin-adduct Protein cysteines can become chemical attachment sites. Incubating purified human cofilin 1 with cucurbitacin E produced covalent adducts; mass shifts were compatible with about four compound molecules per cofilin under the tested excess-compound conditions. Model: Purified human cofilin 1, 5 micromolar; up to 1:100 protein:compound molar ratio, 16 hours. Limitations: Long, high-excess biochemical incubation; does not establish selectivity or occupancy after human ingestion. Evidence access: Primary full text PMC3751690 Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23945128/ · DOI 10.1186/1478-811X-11-58
    Complete structured claim and evidence

  2. Cucurbitacin E pretreatment inhibited the F-actin-severing activity of purified human cofilin 1.

    Cucurbitacin E → Human cofilin-mediated F-actin severing source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC3751690
    experimental_model
    Purified-protein functional assay.
    limitations
    Actin preparation species is not resolved in this record; broad thiol reactivity prevents assigning cofilin as the exclusive cellular target.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Modifying the cutting protein slows filament disassembly.
    primary_references
    Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23945128/ · DOI 10.1186/1478-811X-11-58

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 44–50

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified-protein functional assay. · source_derived_draft · unverified_draft

    ## cucurbitacin-e-cofilin-severing Modifying the cutting protein slows filament disassembly. Cucurbitacin E pretreatment inhibited the F-actin-severing activity of purified human cofilin 1. Model: Purified-protein functional assay. Limitations: Actin preparation species is not resolved in this record; broad thiol reactivity prevents assigning cofilin as the exclusive cellular target. Evidence access: Primary full text PMC3751690 Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23945128/ · DOI 10.1186/1478-811X-11-58
    Complete structured claim and evidence

  3. Mass spectrometry localized cucurbitacin E modification to cofilin Cys39, Cys80 and Cys139, with weaker evidence for Cys147.

    Cucurbitacin E → Human cofilin 1 / CFL1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC3751690
    experimental_model
    Purified human cofilin 1 biochemical mapping.
    limitations
    A protein cysteine residue is not equivalent to free dietary cysteine; these data do not quantify nutritional depletion.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    The study identifies individual protein attachment sites.
    primary_references
    Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23945128/ · DOI 10.1186/1478-811X-11-58

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 36–42

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human cofilin 1 biochemical mapping. · source_derived_draft · unverified_draft

    ## cucurbitacin-e-cofilin-sites The study identifies individual protein attachment sites. Mass spectrometry localized cucurbitacin E modification to cofilin Cys39, Cys80 and Cys139, with weaker evidence for Cys147. Model: Purified human cofilin 1 biochemical mapping. Limitations: A protein cysteine residue is not equivalent to free dietary cysteine; these data do not quantify nutritional depletion. Evidence access: Primary full text PMC3751690 Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23945128/ · DOI 10.1186/1478-811X-11-58
    Complete structured claim and evidence

  4. Cucurbitacin E covalently modified actin at Cys257 in F-actin and inhibited depolymerization, with effects at substoichiometric compound:actin ratios down to 1:6.

    Cucurbitacin E → Purified F-actin in cucurbitacin assays, species as reported source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified actin and cellular photoactivation experiments.
    limitations
    Purified actin species/isoform not established from the accessed abstract; not automatically human ACTB. This study did not find an effect on polymerization.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    The filament itself can be stabilized.
    primary_references
    The natural product cucurbitacin E inhibits depolymerization of actin filaments. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22724897/ · DOI 10.1021/cb300254s

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 52–58

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified actin and cellular photoactivation experiments. · source_derived_draft · unverified_draft

    ## cucurbitacin-e-f-actin The filament itself can be stabilized. Cucurbitacin E covalently modified actin at Cys257 in F-actin and inhibited depolymerization, with effects at substoichiometric compound:actin ratios down to 1:6. Model: Purified actin and cellular photoactivation experiments. Limitations: Purified actin species/isoform not established from the accessed abstract; not automatically human ACTB. This study did not find an effect on polymerization. Evidence access: Primary abstract The natural product cucurbitacin E inhibits depolymerization of actin filaments. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22724897/ · DOI 10.1021/cb300254s
    Complete structured claim and evidence

  5. The cucurbitacin E actin study reported binding to filamentous actin but not globular actin.

    Cucurbitacin E → Purified G-actin in cucurbitacin assays, species as reported source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Same purified-actin experiments.
    limitations
    Member-specific assay result; cannot be transferred to cucurbitacin I.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    The physical state of the protein changes the result.
    primary_references
    The natural product cucurbitacin E inhibits depolymerization of actin filaments. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22724897/ · DOI 10.1021/cb300254s

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 60–66

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Same purified-actin experiments. · source_derived_draft · unverified_draft

    ## cucurbitacin-e-no-g-actin-binding The physical state of the protein changes the result. The cucurbitacin E actin study reported binding to filamentous actin but not globular actin. Model: Same purified-actin experiments. Limitations: Member-specific assay result; cannot be transferred to cucurbitacin I. Evidence access: Primary abstract The natural product cucurbitacin E inhibits depolymerization of actin filaments. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22724897/ · DOI 10.1021/cb300254s
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. At equal oral formulation doses, nanosuspension increased measured peak concentration and exposure area for cucurbitacins B, D and E in rats.

    Rat oral cucurbitacin nanosuspension formulation → Cucurbitacin B source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    2025 rat pharmacokinetic formulation comparison; dose not specified in accessed abstract.
    limitations
    Does not establish human bioavailability or improved clinical safety.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Changing the formulation changed exposure to each member.
    primary_references
    Comparison of the pharmacokinetic profiles of three triterpenoids after oral administration of a cucurbitacin tablet and nanosuspension by UHPLC-MS/MS. · 2025 · https://pubmed.ncbi.nlm.nih.gov/41001343/ · DOI 10.3389/fphar.2025.1647015
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 388–394

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · 2025 rat pharmacokinetic formulation comparison; dose not specified in accessed abstract. · source_derived_draft · unverified_draft

    ## cucurbitacin-formulation-exposure Changing the formulation changed exposure to each member. At equal oral formulation doses, nanosuspension increased measured peak concentration and exposure area for cucurbitacins B, D and E in rats. Model: 2025 rat pharmacokinetic formulation comparison; dose not specified in accessed abstract. Limitations: Does not establish human bioavailability or improved clinical safety. Evidence access: Primary abstract Comparison of the pharmacokinetic profiles of three triterpenoids after oral administration of a cucurbitacin tablet and nanosuspension by UHPLC-MS/MS. · 2025 · https://pubmed.ncbi.nlm.nih.gov/41001343/ · DOI 10.3389/fphar.2025.1647015
    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