<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <id type="integer">1195</id>
  <title>T3D1191</title>
  <common-name>Copper(II) fluoride</common-name>
  <description>Copper(II) fluoride is an exogenous inorganic compound with the formula $\text{CuF}_2$ and an average molecular weight of 101.54 g/mol. It exists as a solid at room temperature and is classified as a mixed metal/non-metal compound. Copper(II) fluoride belongs to the transition metal fluorides, a subclass of transition metal salts within the inorganic compounds. The compound is found in or released from eight recorded sources, including household cleaning and consumer products such as pipe accessories, as well as electrical and electronic equipment including magnets, discharge lamps, emergency protective devices, communication cables or conductors, and power cables.

The compound interacts with six recorded protein targets. Copper binds to alpha-synuclein (SNCA), which initiates protein aggregation and likely contributes to the development of Alzheimer's disease and Parkinson's disease. It also binds the N-terminal region of amyloid-beta precursor protein (APP), promoting the generation of $\beta$-amyloid, which is believed to contribute to these same neurodegenerative disorders. Additionally, copper inhibits sulfhydryl group enzymes including serum paraoxonase/lactonase 3 (PON3), serum paraoxonase/arylesterase 1 (PON1), mitochondrial glutathione reductase (GSR), and glucose-6-phosphate 1-dehydrogenase (G6PD), all of which protect the cell from free oxygen. Copper hepatotoxicity is believed to occur when hepatocyte lysosomes, where excess copper is complexed with metallothionein, become saturated. This leads to copper accumulation in the nucleus and subsequent nuclear damage, possibly resulting from oxidative damage such as lipid peroxidation.</description>
  <cas>7789-19-7</cas>
  <pubchem-id>82236</pubchem-id>
  <chemical-formula>CuF2</chemical-formula>
  <weight>100.926410</weight>
  <appearance>White powder.</appearance>
  <melting-point>836°C</melting-point>
  <boiling-point>1676°C</boiling-point>
  <density nil="true"/>
  <solubility></solubility>
  <specific-gravity nil="true"/>
  <flash-point nil="true"/>
  <vapour-pressure nil="true"/>
  <route-of-exposure>Oral  (L277) ; inhalation  (L277) ; dermal (L277)</route-of-exposure>
  <target nil="true"/>
  <mechanism-of-toxicity>Excess copper is sequestered within hepatocyte lysosomes, where it is complexed with metallothionein. Copper hepatotoxicity is believed to occur when the lysosomes become saturated and copper accumulates in the nucleus, causing nuclear damage. This damage is possibly a result of oxidative damage, including lipid peroxidation. Copper inhibits the sulfhydryl group enzymes such as glucose-6-phosphate 1-dehydrogenase, glutathione reductase, and paraoxonases, which protect the cell from free oxygen radicals. It also influences gene expression and is a co-factor for oxidative enzymes such as cytochrome C oxidase and lysyl oxidase. In addition, the oxidative stress induced by copper is thought to activate acid sphingomyelinase, which lead to the production of ceramide, an apoptotic signal, as well as cause hemolytic anemia. Copper-induced emesis results from stimulation of the vagus nerve. (L277, T49, A174, L280)</mechanism-of-toxicity>
  <metabolism>Copper is mainly absorbed through the gastrointestinal tract, but it can also be inhalated and absorbed dermally. It passes through the basolateral membrane, possibly via regulatory copper transporters, and is transported to the liver and kidney bound to serum albumin. The liver is the critical organ for copper homoeostasis. In the liver and other tissues, copper is stored bound to metallothionein, amino acids, and in association with copper-dependent enzymes, then partitioned for excretion through the bile or incorporation into intra- and extracellular proteins. The transport of copper to the peripheral tissues is accomplished through the plasma attached to serum albumin, ceruloplasmin or low-molecular-weight complexes. Copper may induce the production of metallothionein and ceruloplasmin. The membrane-bound copper transporting adenosine triphosphatase (Cu-ATPase) transports copper ions into and out of cells. Physiologically normal levels of copper in the body are held constant by alterations in the rate and amount of copper absorption, compartmental distribution, and excretion. (L277, L279)</metabolism>
  <toxicity nil="true"/>
  <lethaldose>10 to 20 grams for an adult human (copper salts). (T17)</lethaldose>
  <carcinogenicity>No indication of carcinogenicity to humans (not listed by IARC).</carcinogenicity>
  <use-source nil="true"/>
  <min-risk-level>Acute Oral: 0.01 mg/kg/day (L134) 
Intermediate Oral: 0.01 mg/kg/day (L134)</min-risk-level>
  <health-effects>People must absorb small amounts of copper every day because copper is essential for good health, however, high levels of copper can be harmful. Very-high doses of copper can cause damage to your liver and kidneys, and can even cause death. Copper may induce allergic responses in sensitive individuals. (L278, L279)</health-effects>
  <symptoms>Breathing high levels of copper can cause irritation of the nose and throat. Ingesting high levels of copper can cause nausea, vomiting, diarrhea, headache, dizziness, and respiratory difficulty. (L278, L279)</symptoms>
  <treatment>EYES: irrigate opened eyes for several minutes under running water. INGESTION: do not induce vomiting. Rinse mouth with water (never give anything by mouth to an unconscious person). Seek immediate medical advice. SKIN: should be treated immediately by rinsing the affected parts in cold running water for at least 15 minutes, followed by thorough washing with soap and water. If necessary, the person should shower and change contaminated clothing and shoes, and then must seek medical attention. INHALATION: supply fresh air. If required provide artificial respiration.</treatment>
  <created-at type="dateTime">2009-06-19T21:58:25Z</created-at>
  <updated-at type="dateTime">2026-08-26T00:23:36Z</updated-at>
  <interacting-proteins>High affinity copper uptake protein 1 (O15431) Probable low affinity copper uptake protein 2 (O15432) Serum albumin (P02768) Ceruloplasmin (P00450) Copper-transporting ATPase 1 (Q04656) Copper-transporting ATPase 2 (P35670) Copper transport protein ATOX1 (O00244) Copper chaperone for superoxide dismutase (O14618) Cytochrome c oxidase copper chaperone (Q14061) Metallothionein-2 (P02795) Metallothionein-1G (P13640) Metallothionein-1H (P80294) Metallothionein-3 (P25713) Metallothionein-1F (P04733) Metallothionein-1E (P04732) Metallothionein-1X (P80297) Metallothionein-1A (P04731) Metallothionein-1B (P07438) Metallothionein-1M (Q8N339) Metallothionein-4 (P47944) Metallothionein-1L (Q93083) (L277, A176)</interacting-proteins>
  <wikipedia nil="true"/>
  <uniprot-id nil="true"/>
  <kegg-compound-id></kegg-compound-id>
  <omim-id></omim-id>
  <chebi-id></chebi-id>
  <biocyc-id></biocyc-id>
  <ctd-id>C057829</ctd-id>
  <stitch-id>Copper(II) fluoride</stitch-id>
  <drugbank-id nil="true"/>
  <pdb-id nil="true"/>
  <actor-id nil="true"/>
  <organism nil="true"/>
  <export type="boolean">true</export>
  <metabolizing-proteins nil="true"/>
  <transporting-proteins>High affinity copper uptake protein 1 (O15431) 
Probable low affinity copper uptake protein 2 (O15432) 
Serum albumin (P02768) 
Ceruloplasmin (P00450) 
Copper-transporting ATPase 1 (Q04656) 
Copper-transporting ATPase 2 (P35670) 
Copper transport protein ATOX1 (O00244) 
Copper chaperone for superoxide dismutase (O14618) 
Cytochrome c oxidase copper chaperone (Q14061) 
Metallothionein-2 (P02795) 
Metallothionein-1G (P13640) 
Metallothionein-1H (P80294) 
Metallothionein-3 (P25713) 
Metallothionein-1F (P04733) 
Metallothionein-1E (P04732) 
Metallothionein-1X (P80297) 
Metallothionein-1A (P04731) 
Metallothionein-1B (P07438) 
Metallothionein-1M (Q8N339) 
Metallothionein-4 (P47944) 
Metallothionein-1L (Q93083) 
(L277, A176)</transporting-proteins>
  <moldb-smiles>F[Cu]F</moldb-smiles>
  <moldb-formula>CuF2</moldb-formula>
  <moldb-inchi>InChI=1S/Cu.2FH/h;2*1H/q+2;;/p-2</moldb-inchi>
  <moldb-inchikey>GWFAVIIMQDUCRA-UHFFFAOYSA-L</moldb-inchikey>
  <moldb-average-mass type="decimal">101.543</moldb-average-mass>
  <moldb-mono-mass type="decimal">100.926407489</moldb-mono-mass>
  <origin>Exogenous</origin>
  <state>Solid</state>
  <logp nil="true"/>
  <hmdb-id nil="true"/>
  <chembl-id nil="true"/>
  <chemspider-id>74214</chemspider-id>
  <structure-image-file-name nil="true"/>
  <structure-image-content-type nil="true"/>
  <structure-image-file-size type="integer" nil="true"/>
  <structure-image-updated-at type="dateTime" nil="true"/>
  <biodb-id nil="true"/>
  <synthesis-reference></synthesis-reference>
  <structure-image-caption nil="true"/>
  <chemdb-id>CHEM001020</chemdb-id>
  <dsstox-id nil="true"/>
  <toxcast-id nil="true"/>
  <stoff-ident-origin nil="true"/>
  <stoff-ident-id nil="true"/>
  <susdat-id>NS00080836</susdat-id>
  <iupac>difluorocopper</iupac>
  <moldb-polar-surface-area>0</moldb-polar-surface-area>
  <moldb-refractivity>3.0026</moldb-refractivity>
  <moldb-polarizability>2.7680639048205373</moldb-polarizability>
  <moldb-rotatable-bond-count>0</moldb-rotatable-bond-count>
  <moldb-acceptor-count>0</moldb-acceptor-count>
  <moldb-donor-count>0</moldb-donor-count>
  <moldb-pka-strongest-acidic nil="true"/>
  <moldb-pka-strongest-basic nil="true"/>
  <moldb-physiological-charge>0</moldb-physiological-charge>
  <moldb-number-of-rings>0</moldb-number-of-rings>
  <moldb-alogps-logp nil="true"/>
  <moldb-alogps-logs nil="true"/>
  <moldb-alogps-solubility nil="true"/>
  <kingdom>Inorganic compounds</kingdom>
  <superklass>Mixed metal/non-metal compounds</superklass>
  <klass>Transition metal salts</klass>
  <subklass>Transition metal fluorides</subklass>
  <paper-count type="integer">70</paper-count>
  <sync-id>CED0001967</sync-id>
  <structure-inchikey>GWFAVIIMQDUCRA-UHFFFAOYSA-L</structure-inchikey>
  <structure-fingerprint>1000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000800000000000000000000000001000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000800000000000000000000000000000</structure-fingerprint>
  <structure-pattern-fingerprint>4000000000040000000000000000000000000000000000000000000000000000400000000000000000000000000000000008000000000000200000000000000020000000000000000000000000000000000000000000000000000000000000000000001000000000000020040000004000000000000000000000000000000002000000000080000000000008008000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000000</structure-pattern-fingerprint>
  <structure-pickle type="binary" encoding="base64">776t3gAAAAAQAAAAAwAAAAAAAAADAAAAAgAAAIABCQAgAAAAAR0gKAAAAAcC
CQAgAAAAAQsAAQABAgBCAAAAABcEAAAAAAAAABY=
</structure-pickle>
  <structure-indexed-at type="dateTime">2026-09-19T04:00:01Z</structure-indexed-at>
</compound>
