Phalloidin
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Basic Info
| Common Name | Phalloidin(F04694) |
| 2D Structure | |
| Description | Phalloidin is one of a group of toxins from the Amanita phalloides known as phallotoxins. Though highly toxic to liver cells, it has since been found to have little input into the Amanita phalloides's toxicity as it is not absorbed through the gut. Furthermore, it is also found in the edible Blusher (Amanita rubescens). |
| FRCD ID | F04694 |
| CAS Number | 17466-45-4 |
| PubChem CID | 4752 |
| Formula | C35H48N8O11S |
| IUPAC Name | None |
| InChI Key | KPKZJLCSROULON-UHFFFAOYSA-N |
| InChI | InChI=1S/C35H48N8O11S/c1-15-27(47)38-22-10-20-19-7-5-6-8-21(19)41-33(20)55-13-24(34(53)43-12-18(46)9-25(43)31(51)37-15)40-32(52)26(17(3)45)42-28(48)16(2)36-30(50)23(39-29(22)49)11-35(4,54)14-44/h5-8,15-18,22-26,41,44-46,54H,9-14H2,1-4H3,(H,36,50)(H,37,51)(H,38,47)(H,39,49)(H,40,52)(H,42,48) |
| Canonical SMILES | CC1C(=O)NC2CC3=C(NC4=CC=CC=C34)SCC(C(=O)N5CC(CC5C(=O)N1)O)NC(=O)C(NC(=O)C(NC(=O)C(NC2=O)CC(C)(CO)O)C)C(C)O |
| Isomeric SMILES | CC1C(=O)NC2CC3=C(NC4=CC=CC=C34)SCC(C(=O)N5CC(CC5C(=O)N1)O)NC(=O)C(NC(=O)C(NC(=O)C(NC2=O)CC(C)(CO)O)C)C(C)O |
| Wikipedia | Phalloidin |
| Synonyms |
28-(2,3-dihydroxy-2-methylpropyl)-18-hydroxy-34-(1-hydroxyethyl)-23,31-dimethyl-12-thia-10,16,22,25,27,30,33,36-octaazapentacyclo[12.11.11.03,11.04,9.016,20]hexatriaconta-3(11),4,6,8-tetraene-15,21,24,26,29,32,35-heptone
PHALLOIDIN
17466-45-4
HSDB 3524
EINECS 241-484-5
NSC 523214
BRN 4347460
AC1L1IVH
AC1Q6LQW
D0I9YJ
|
| Classifies |
Fungal Toxin
|
| Update Date | Nov 13, 2018 17:07 |
Chemical Taxonomy
| Kingdom | Organic compounds |
| Superclass | Organic acids and derivatives |
| Class | Carboxylic acids and derivatives |
| Subclass | Amino acids, peptides, and analogues |
| Intermediate Tree Nodes | Peptides |
| Direct Parent | Oligopeptides |
| Alternative Parents |
|
| Molecular Framework | Aromatic heteropolycyclic compounds |
| Substituents | Alpha-oligopeptide - Cyclic alpha peptide - Macrolactam - Alpha-amino acid or derivatives - 3-alkylindole - Indole - Indole or derivatives - Aryl thioether - Alkylarylthioether - Benzenoid - Heteroaromatic compound - Pyrrole - Pyrrolidine - Tertiary alcohol - Tertiary carboxylic acid amide - Carboxamide group - Lactam - Secondary alcohol - Secondary carboxylic acid amide - Azacycle - Organoheterocyclic compound - Thioether - Primary alcohol - Organooxygen compound - Organonitrogen compound - Hydrocarbon derivative - Organic nitrogen compound - Organic oxide - Organopnictogen compound - Organic oxygen compound - Alcohol - Carbonyl group - Aromatic heteropolycyclic compound |
| Description | This compound belongs to the class of organic compounds known as oligopeptides. These are organic compounds containing a sequence of between three and ten alpha-amino acids joined by peptide bonds. |
Properties
| Property Name | Property Value |
|---|---|
| Molecular Weight | 788.874 |
| Hydrogen Bond Donor Count | 11 |
| Hydrogen Bond Acceptor Count | 12 |
| Rotatable Bond Count | 4 |
| Complexity | 1510 |
| Monoisotopic Mass | 788.316 |
| Exact Mass | 788.316 |
| XLogP | -1.7 |
| Formal Charge | 0 |
| Heavy Atom Count | 55 |
| Defined Atom Stereocenter Count | 0 |
| Undefined Atom Stereocenter Count | 10 |
| Defined Bond Stereocenter Count | 0 |
| Undefined Bond Stereocenter Count | 0 |
| Isotope Atom Count | 0 |
| Covalently-Bonded Unit Count | 1 |
ADMET
| Model | Result | Probability |
|---|---|---|
| Absorption | ||
| Blood-Brain Barrier | BBB- | 0.9675 |
| Human Intestinal Absorption | HIA+ | 0.6387 |
| Caco-2 Permeability | Caco2- | 0.7625 |
| P-glycoprotein Substrate | Substrate | 0.7966 |
| P-glycoprotein Inhibitor | Non-inhibitor | 0.8778 |
| Non-inhibitor | 0.9457 | |
| Renal Organic Cation Transporter | Non-inhibitor | 0.9419 |
| Distribution | ||
| Subcellular localization | Mitochondria | 0.4800 |
| Metabolism | ||
| CYP450 2C9 Substrate | Non-substrate | 0.8059 |
| CYP450 2D6 Substrate | Non-substrate | 0.7308 |
| CYP450 3A4 Substrate | Substrate | 0.5435 |
| CYP450 1A2 Inhibitor | Non-inhibitor | 0.7663 |
| CYP450 2C9 Inhibitor | Non-inhibitor | 0.7785 |
| CYP450 2D6 Inhibitor | Non-inhibitor | 0.8737 |
| CYP450 2C19 Inhibitor | Non-inhibitor | 0.6858 |
| CYP450 3A4 Inhibitor | Non-inhibitor | 0.7894 |
| CYP Inhibitory Promiscuity | Low CYP Inhibitory Promiscuity | 0.6662 |
| Excretion | ||
| Toxicity | ||
| Human Ether-a-go-go-Related Gene Inhibition | Weak inhibitor | 0.9977 |
| Non-inhibitor | 0.6669 | |
| AMES Toxicity | Non AMES toxic | 0.7061 |
| Carcinogens | Non-carcinogens | 0.7599 |
| Fish Toxicity | High FHMT | 0.8946 |
| Tetrahymena Pyriformis Toxicity | High TPT | 0.9534 |
| Honey Bee Toxicity | Low HBT | 0.6844 |
| Biodegradation | Not ready biodegradable | 1.0000 |
| Acute Oral Toxicity | III | 0.5627 |
| Carcinogenicity (Three-class) | Non-required | 0.5773 |
| Model | Value | Unit |
|---|---|---|
| Absorption | ||
| Aqueous solubility | -2.8450 | LogS |
| Caco-2 Permeability | 0.2889 | LogPapp, cm/s |
| Distribution | ||
| Metabolism | ||
| Excretion | ||
| Toxicity | ||
| Rat Acute Toxicity | 2.4984 | LD50, mol/kg |
| Fish Toxicity | 1.6446 | pLC50, mg/L |
| Tetrahymena Pyriformis Toxicity | 0.3383 | pIGC50, ug/L |
References
| Title | Journal | Date | Pubmed ID |
|---|---|---|---|
| A Simple and High-Throughput Analysis of Amatoxins and Phallotoxins in Human Plasma, Serum and Urine Using UPLC-MS/MS Combined with PRiME HLB μElution Platform. | Toxins (Basel) | 2016 May 4 | 27153089 |
| Antiobesity Action of ACAM by Modulating the Dynamics of Cell Adhesion and Actin Polymerization in Adipocytes. | Diabetes | 2016 May | 26956488 |
| Exogenous phosphatidylcholine supplementation improves intestinal barrier defense against Clostridium difficile toxin. | J Trauma Acute Care Surg | 2014 Oct | 25250596 |
| Ghrelin promotes reorganization of dendritic spines in cultured rat hippocampal slices. | Neurosci Lett | 2012 May 16 | 22516464 |
| [A fluorimetric microplate assay for detecting diarrheic shellfish poisoning toxins]. | Wei Sheng Yan Jiu | 2012 May | 23050458 |
| Dimethylarsinous acid disturbs cytokinesis. | Bull Environ Contam Toxicol | 2009 Jul | 19319459 |
| Effects of a synthetic analog of polycavernoside A on human neuroblastoma cells. | Cell Physiol Biochem | 2007 | 17310112 |
| A comparison of F-actin labeling methods for light microscopy in different plant specimens: multiple techniques supplement each other. | Micron | 2001 Aug | 11166577 |
| Effect of dietary lipid (soybean lecithin and triacylglycerol) on hepatic F-actin microfilaments in cyclosporine A-treated rats: image analysis by confocal laser scanning microscopy. | Dig Dis Sci | 2000 Jun | 10877222 |
| Differential dynamic behavior of actin filaments containing tightly-bound Ca2+ or Mg2+ in the presence of myosin heads actively hydrolyzing ATP. | Biochemistry | 1999 Oct 5 | 10529203 |
| Influence of tightly bound Mg2+ and Ca2+, nucleotides, and phalloidin on the microsecond torsional flexibility of F-actin. | Biochemistry | 1998 Oct 13 | 9772181 |
| A giant nerve net with multi-effector synapses underlying epithelial adhesive strips in the mouth of Beroë (Ctenophora). | J Neurocytol | 1995 Sep | 7500125 |
| Electron spin resonance studies of fatty acid-induced alterations in membrane fluidity in cultured endothelial cells. | Int J Biochem Cell Biol | 1995 Jul | 7648422 |
| Rhodamine-labelled phalloidin stains components in the chromosomal spindle fibres of crane-fly spermatocytes and Haemanthus endosperm cells. | Biochem Cell Biol | 1992 Aug | 1282338 |
| Inhibition by the mushroom toxins alpha-amanitin and phalloidin of hepatopoietin-induced 3H-thymidine incorporation into rat liver DNA and of plasma protein production in hepatocyte cultures. | Toxicon | 1987 | 3326217 |
| Filamentous actin in Paramecium cells: mapping by phalloidin affinity labeling in vivo and in vitro. | J Histochem Cytochem | 1986 Apr | 2419395 |
| Filamentous actin in paramecium cells: functional and structural changes correlated with phalloidin affinity labeling in vivo. | J Histochem Cytochem | 1986 Apr | 3512697 |
| Antihepatoxic constituents of Garcinia kola seeds. | Experientia | 1985 May 15 | 3838940 |
| [Effect of silymarin on the isolated perfused rat liver poisoned by phalloidin]. | Arzneimittelforschung | 1970 Jun | 5468908 |
| [Electron microscopic studies on the Phalloidin tolerance of newborn rats, mice and rabbits]. | Virchows Arch B Cell Pathol | 1970 | 4990260 |
Targets
- General Function:
- Structural constituent of cytoskeleton
- Specific Function:
- Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
- Gene Name:
- ACTA1
- Uniprot ID:
- P68133
- Molecular Weight:
- 42050.67 Da
- Mechanism of Action:
- Phallotoxins bind actin, preventing its depolymerization and poisoning the cell. They bind specifically at the interface between F-actin subunits, locking adjacent subunits together. This leads to a decrease in the rate constant for the dissociation of actin subunits from filament ends, which essentially stabilizes actin filaments through the prevention of filament depolymerization. Moreover, they inhibit the ATP hydrolysis activity of F-actin.
References
- Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
- General Function:
- Tat protein binding
- Specific Function:
- Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
- Gene Name:
- ACTB
- Uniprot ID:
- P60709
- Molecular Weight:
- 41736.37 Da
- Mechanism of Action:
- Phallotoxins bind actin, preventing its depolymerization and poisoning the cell. They bind specifically at the interface between F-actin subunits, locking adjacent subunits together. This leads to a decrease in the rate constant for the dissociation of actin subunits from filament ends, which essentially stabilizes actin filaments through the prevention of filament depolymerization. Moreover, they inhibit the ATP hydrolysis activity of F-actin.
References
- Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
- General Function:
- Ubiquitin protein ligase binding
- Specific Function:
- Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
- Gene Name:
- ACTG1
- Uniprot ID:
- P63261
- Molecular Weight:
- 41792.48 Da
- Mechanism of Action:
- Phallotoxins bind actin, preventing its depolymerization and poisoning the cell. They bind specifically at the interface between F-actin subunits, locking adjacent subunits together. This leads to a decrease in the rate constant for the dissociation of actin subunits from filament ends, which essentially stabilizes actin filaments through the prevention of filament depolymerization. Moreover, they inhibit the ATP hydrolysis activity of F-actin.
References
- Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
- General Function:
- Atp binding
- Specific Function:
- Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
- Gene Name:
- ACTG2
- Uniprot ID:
- P63267
- Molecular Weight:
- 41876.495 Da
- Mechanism of Action:
- Phallotoxins bind actin, preventing its depolymerization and poisoning the cell. They bind specifically at the interface between F-actin subunits, locking adjacent subunits together. This leads to a decrease in the rate constant for the dissociation of actin subunits from filament ends, which essentially stabilizes actin filaments through the prevention of filament depolymerization. Moreover, they inhibit the ATP hydrolysis activity of F-actin.
References
- Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
- General Function:
- Myosin binding
- Specific Function:
- Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
- Gene Name:
- ACTC1
- Uniprot ID:
- P68032
- Molecular Weight:
- 42018.6 Da
- Mechanism of Action:
- Phallotoxins bind actin, preventing its depolymerization and poisoning the cell. They bind specifically at the interface between F-actin subunits, locking adjacent subunits together. This leads to a decrease in the rate constant for the dissociation of actin subunits from filament ends, which essentially stabilizes actin filaments through the prevention of filament depolymerization. Moreover, they inhibit the ATP hydrolysis activity of F-actin.
References
- Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]
- General Function:
- Protein kinase binding
- Specific Function:
- Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
- Gene Name:
- ACTA2
- Uniprot ID:
- P62736
- Molecular Weight:
- 42008.57 Da
- Mechanism of Action:
- Phallotoxins bind actin, preventing its depolymerization and poisoning the cell. They bind specifically at the interface between F-actin subunits, locking adjacent subunits together. This leads to a decrease in the rate constant for the dissociation of actin subunits from filament ends, which essentially stabilizes actin filaments through the prevention of filament depolymerization. Moreover, they inhibit the ATP hydrolysis activity of F-actin.
References
- Huang ZJ, Haugland RP, You WM, Haugland RP: Phallotoxin and actin binding assay by fluorescence enhancement. Anal Biochem. 1992 Jan;200(1):199-204. [1595896 ]