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TMTFA

From Wikipedia, the free encyclopedia
Chemical compound
TMTFA
Names
Preferred IUPAC name
N,N,N-Trimethyl-3-(trifluoroacetyl)anilinium
Identifiers
3D model (JSmol)
ChemSpider
UNII
  • InChI=1S/C11H13F3NO/c1-15(2,3)9-6-4-5-8(7-9)10(16)11(12,13)14/h4-7H,1-3H3/q+1
    Key: JIBZSTPMDKSJOX-UHFFFAOYSA-N
  • C[N+](C)(C)C1=CC=CC(=C1)C(=O)C(F)(F)F
Properties
C11H13F3NO
Molar mass232.226 g·mol−1
Hazards
Lethal dose or concentration (LD, LC):
1.6 mg/kg (intraperitoneal, mice) (as iodide salt)[1]
Except where otherwise noted, data are given for materials in theirstandard state (at 25 °C [77 °F], 100 kPa).
Chemical compound

TMTFA is an extremely potentacetylcholinesterase inhibitor. As atransition state analog ofacetylcholinesterase, TMTFA is able to inhibit acetylcholinesterase at extremely low concentrations (within thefemtomolar range), making it one of the most potent acetylcholinesterase inhibitors known.[2][3][4]

Mechanism of action

[edit]

TMTFA has a reactiveketone group that can covalently bind to theserine residue in the active site of acetylcholinesterase. This is due to the electron-withdrawingtrifluoromethyl group on thecarbonyl group.[5]

See also

[edit]

References

[edit]
  1. ^Brodbeck, U.; Schweikert, K.; Gentinetta, R.; Rottenberg, M. (April 1979). "Fluorinated aldehydes and ketones acting as quasi-substrate inhibitors of acetylcholinesterase".Biochimica et Biophysica Acta (BBA) - Enzymology.567 (2):357–369.doi:10.1016/0005-2744(79)90122-0.PMID 444532.
  2. ^Nair, Haridasan K.; Lee, Keun; Quinn, Daniel M. (November 1993). "m-(N,N,N-Trimethylammonio)trifluoroacetophenone: a femtomolar inhibitor of acetylcholinesterase".Journal of the American Chemical Society.115 (22):9939–9941.Bibcode:1993JAChS.115.9939N.doi:10.1021/ja00075a009.
  3. ^Kua, Jeremy; Zhang, Yingkai; McCammon, J. Andrew (2002). "Studying Enzyme Binding Specificity in Acetylcholinesterase Using a Combined Molecular Dynamics and Multiple Docking Approach".Journal of the American Chemical Society.124 (28):8260–8267.Bibcode:2002JAChS.124.8260K.doi:10.1021/ja020429l.PMID 12105904.
  4. ^Butini, Stefania; Campiani, Giuseppe; Borriello, Marianna; Gemma, Sandra; Panico, Alessandro; Persico, Marco; Catalanotti, Bruno; Ros, Sindu; Brindisi, Margherita; Agnusdei, Marianna; Fiorini, Isabella; Nacci, Vito; Novellino, Ettore; Belinskaya, Tatyana; Saxena, Ashima; Fattorusso, Caterina (2008). "Exploiting Protein Fluctuations at the Active-Site Gorge of Human Cholinesterases: Further Optimization of the Design Strategy to Develop Extremely Potent Inhibitors".Journal of Medicinal Chemistry.51 (11):3154–3170.doi:10.1021/jm701253t.PMID 18479118.
  5. ^Harel, Michal; Quinn, Daniel M.; Nair, Haridasan K.; Silman, Israel; Sussman, Joel L. (January 1996). "The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase".Journal of the American Chemical Society.118 (10):2340–2346.Bibcode:1996JAChS.118.2340H.doi:10.1021/ja952232h.
Enzyme
(modulators)
ChATTooltip Choline acetyltransferase
AChETooltip Acetylcholinesterase
BChETooltip Butyrylcholinesterase
Transporter
(modulators)
CHTTooltip Choline transporter
VAChTTooltip Vesicular acetylcholine transporter
Release
(modulators)
Inhibitors
Enhancers
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