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Tandem mass spectrometric data-FAAH inhibitory activity relationships of some carbamic acid O-aryl esters
Journal of mass spectrometry, 2004-12, Vol.39 (12), p.1450-1455
Basso, Elisa
Duranti, Andrea
Mor, Marco
Piomelli, Daniele
Tontini, Andrea
Tarzia, Giorgio
Traldi, Pietro
2004
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Basso, Elisa
Duranti, Andrea
Mor, Marco
Piomelli, Daniele
Tontini, Andrea
Tarzia, Giorgio
Traldi, Pietro
Titel
Tandem mass spectrometric data-FAAH inhibitory activity relationships of some carbamic acid O-aryl esters
Ist Teil von
Journal of mass spectrometry, 2004-12, Vol.39 (12), p.1450-1455
Ort / Verlag
Chichester, UK: John Wiley & Sons, Ltd
Erscheinungsjahr
2004
Quelle
MEDLINE
Beschreibungen/Notizen
We have recently described a class of systemically active inhibitors of the intracellular activity of fatty acid amide hydrolase (FAAH) and traced extensive structure–activity relationships. These compounds, characterized by an N‐alkyl carbamic acid O‐aryl ester structure, exert potent anxiolytic‐like effects in animal models. In the present study, possible relationships between mass spectrometric parameters (related to the propensity of the C(O)O bond to be cleaved) and FAAH‐inhibitory potency were tested. With this aim, a set of our products was analyzed by electrospray ionization mass spectrometry and the protonated molecules were decomposed by low‐energy collisions. The experiments were performed by ion trap mass spectrometry, which led to a step‐by‐step energy deposition, thus favouring the lowest critical energy decomposition channels. For all compounds, breakdown curves relative to [MH]+ ions and to the fragment implying C(O)O bond cleavage were obtained. The crossing point between these curves was related to the energetics of decomposition and the values found for the investigated compounds were linearly correlated (r2 = 0.797) with their FAAH‐inhibitory activity. This indicates that the energetics of the C(O)O bond cleavage may be relevant in explaining FAAH inhibition. Copyright © 2004 John Wiley & Sons, Ltd.
Sprache
Englisch
Identifikatoren
ISSN: 1076-5174
eISSN: 1096-9888
DOI: 10.1002/jms.729
Titel-ID: cdi_proquest_miscellaneous_67185290
Format
–
Schlagworte
Amidohydrolases - antagonists & inhibitors
,
Amidohydrolases - chemistry
,
Biological and medical sciences
,
carbamates
,
Carbamates - chemistry
,
Carbamates - pharmacology
,
Catalytic Domain
,
Enzyme Inhibitors - chemistry
,
Enzyme Inhibitors - pharmacology
,
Esters
,
FAAH inhibitory activity
,
fatty acid amide hydrolase
,
Medical sciences
,
Miscellaneous
,
Pharmacology. Drug treatments
,
Protein Conformation
,
Spectrometry, Mass, Electrospray Ionization - methods
,
tandem mass spectrometry
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