17466-45-4

Basic information

• Product Name: PHALLOIDIN
• Synonyms: pto-l-tryptophyl-4,5-dihydroxy-l-leucyl),cyclic(3,6)-sulfide;PHALLOIDIN;PHALLOIDIN, AMANITA PHALLOIDES;PHALLOIDIN FROM AMANITA PHALLOIDES;Cyclo(L-Ala-D-Thr-L-Cys(1)-L-c4Hyp-L-Ala-L-Trp2(1)-4,5'-dihydroxy-L-Leu-);Cyclic(L-alanyl-D-threonyl-L-cysteinyl-cis-4-hydroxy-L-prolyl-L-alanyl-2-mercapto-L-tryptophyl-4,5-dihydroxy-L-leucyl), cyclic (3.fwdarw.6)-sulfide;Nsc523214;cyclic(l-alanyl-d-threonyl-l-cysteinyl-cis-4-hydroxy-l-prolyl-l-alanyl-2-merca
• CAS NO: 17466-45-4
• Molecular Formula: C₃₅H₄₈N₈O₁₁S
• Molecular Weight: 788.87
• EINECS: 241-484-5
• Product Categories: marker
• Mol File: 17466-45-4.mol
• Article Data: 14

Chemical Properties

• Melting Point: 280-282°
• Boiling Point: 1370.5°Cat760mmHg
• Flash Point: 782.6°C
• Appearance: white powder
• Density: 1.1612 (rough estimate)
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.7400 (estimate)
• Storage Temp.: +2C to +8C
• PKA: 13.03±0.70(Predicted)
• Stability: Stable. Incompatible with strong oxidizing agents.
• Merck: 13,7273
• BRN: 4347460
• CAS DataBase Reference: PHALLOIDIN(CAS DataBase Reference)
• NIST Chemistry Reference: PHALLOIDIN(17466-45-4)
• EPA Substance Registry System: PHALLOIDIN(17466-45-4)

Safety Data

• Hazard Codes: T+
• Statements: 26/27/28
• Safety Statements: 22-28-36/37-45
• RIDADR: UN 3462 6.1/PG 2
• WGK Germany: 3
• RTECS: SE9800000
• F: 18
• HazardClass: 6.1(a)
• PackingGroup: I
• Hazardous Substances Data: 17466-45-4(Hazardous Substances Data)

Usage

Description

Phalloidin is a natural mycotoxin derived from the death cap mushroom, Amanita phalloides. It is a cyclic heptapeptide with a unique crosslink between tryptophan and cysteine, which allows it to interact with actin. This interaction was first identified in phalloidin-poisoned rats. Phalloidin is known for its ability to bind and stabilize F-actin, making it a valuable tool in various applications.

Uses

Used in Research and Diagnostics:
Phalloidin is used as a staining agent in immunohistochemistry for visualizing F-actin in cells. Its ability to bind and stabilize actin fibers makes it an essential tool for studying the cytoskeleton and cellular structure.
Used in Drug Development:
Phalloidin has been explored as a potential drug due to its interaction with actin, which plays a crucial role in various cellular processes. However, its toxicity must be carefully considered in drug development.
Used in Buffer Solutions:
Phalloidin is used as a supplement in PEM buffer and dimethyl sulfoxide (DMSO) to maintain the stability of actin fibers during experiments.
Used in Fluorescent Labeling:
The side chain of amino acid 7 (γ-δ-dihydroxyleucine) in phalloidin is accessible to modifications, allowing the production of fluorescently labeled phalloidin compounds. These labeled compounds are used for visualizing and studying actin dynamics in cells.

Biochem/physiol Actions

Toxin that binds polymeric F actin, stabilizing it and interfering with the function of actin-rich structures.

Safety Profile

Poison by ingestion, intraperitoneal, and intravenous routes. Mutation data reported. Whenheated to decomposition it emits toxic fumes of SOx, and NOx.

Enzyme inhibitor

This bicyclic heptapeptide toxin (FW = 788.88 g/mol; CAS 17466-45-4) is was first isolated from the poisonous green fungus Amanita phalloides. Primary Mode of Action: Phalloidin binds preferentially to filamentous actin; little or no binding to globular actin has been detected. such preferential action stimulates actin polymerization, and phalloidin lowers the actin monomer critical concentration by 30x, from 50-100 nM down to 2-3 nM. When present at 1 to 10 concentration ratio of phalloidin to total actin subunits, actin filaments are also greatly stabilized toward depolymerization. Effects on Actin Filaments: Cellular processes requiring filament disassembly are likewise inhibited. Depolymerization of F-actin by cytochalasins, potassium iodide, and elevated temperatures are inhibited by phalloidin binding. Because the toxin and its fluorescent derivatives are relatively small, a wide variety of actin-binding proteins can still bind to phalloidin-labeled filamentts. Perhaps more significantly, phalloidin-labeled actin filaments retain many of their functional properties, such that phalloidin-labeled, glycerinated muscle fibers can still contract, and labeled actin filaments still move on myosin that has been tethered to solid-phase substrates. Phalloidin can be also be used to assess the relativeconcentrations of these two forms of actin as well as a means to label actin filaments in a cell (See Phallacidin).

InChI:InChI=1/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)/t15-,16-,17-,18-,22-,23-,24-,25-,26+,35+/m0/s1

Upstream product

• 15761-38-3 L-N-Boc-Ala 
• 50-81-7 ascorbic acid 

Downstream Products

• 87876-31-1 N^δ-<4-<(1-Azi-2,2,2-trifluorethyl)benzoyl>-β-alanyl>-δ-aminophalloin 
• 87892-72-6 N^δ-(4-Hexyloxyphenyl)-δ-aminophalloin 
• 87876-23-1 N^δ-Phenyl-δ-aminophalloin 

Related news

The effect on actin ATPase of PHALLOIDIN (cas 17466-45-4) and tetramethylrhodamine PHALLOIDIN (cas 17466-45-4)07/16/2019

Actin polymerization has been studied in the absence of excess nucleotide. Using G-actin ATP monomers, it was shown that mechanical shearing stimulates ATP hydrolysis. The procedures used enabled the detection of differential effects of phalloidin and tetramethylrhodamine-phalloidin, on the Pi-r...detailed

Relevant articles and documents

Total Synthesis of the Death Cap Toxin Phalloidin: Atropoisomer Selectivity Explained by Molecular-Dynamics Simulations

Phallotoxins and amatoxins are a group of prominent peptide toxins produced by the death cap mushroom Amanita phalloides. Phalloidin is a bicyclic cyclopeptide with an unusual tryptathionin thioether bridge. It is a potent stabilizer of filamentous actin and in a fluorescently labeled form widely used as a probe for actin binding. Herein, we report the enantioselective synthesis of the key amino acid (2S,4R)-4,5-dihydroxy-leucine as a basis for the first total synthesis of phalloidin, which was accomplished by two different synthesis strategies. Molecular-dynamics simulations provided insights into the conformational flexibility of peptide intermediates of different reaction strategies and showed that this flexibility is critical for the formation of atropoisomers. By simulating the intermediates, rather than the final product, molecular-dynamics simulations will become a decisive tool in orchestrating the sequence of ring formation reactions of complex cyclic peptides.

Preparation of phalloidin and its derivatives

The present invention relates to novel phalloidin derivatives and their fluorescent dye conjugates. These new compounds may be used in studies of actin dynamics in living systems. The present invention also relates to methods for preparing such compounds. The synthesis routes combine solid-phase and solution phase peptide synthesis, and has great advantage for efficient preparation of a diverse library of the phalloidin derivatives, especially for the synthesis of phalloidin.

XANTHENE DYES COMPRISING A SULFONAMIDE GROUP

The present invention relates to fluorescent dyes in general. The present invention provides a wide range of fluorescent dyes and kits containing the same, which are applicable for labeling a variety of biomolecules, cells and microorganisms. The present invention also provides various methods of using the fluorescent dyes for research and development, forensic identification, environmental studies, diagnosis, prognosis, and/or treatment of disease conditions.