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Probing the steric requirements of the gamma-aminobutyric acid aminotransferase active site with fluorinated analogues of vigabatrin
Journal article   Open access   Peer reviewed

Probing the steric requirements of the gamma-aminobutyric acid aminotransferase active site with fluorinated analogues of vigabatrin

Jose I. Juncosa, Andrew P. Groves, Guoyao Xia and Richard B. Silverman
Bioorganic & medicinal chemistry, Vol.21(4), pp.903-911
02/15/2013
DOI: 10.1016/j.bmc.2012.12.009
PMCID: PMC3563932
PMID: 23306054
url
https://doi.org/10.7270/q2fx7brmView
Open Access

Abstract

We have synthesized three analogues of 4-amino-5-fluorohexanoic acids as potential inactivators of gamma-aminobutyric acid aminotransferase (GABA-AT), which were designed to combine the potency of their shorter chain analogue, 4-amino-5-fluoropentanoic acid (AFPA), with the greater enzyme selectivity of the antiepileptic vigabatrin (Sabril (R)). Unexpectedly, these compounds failed to inactivate or inhibit the enzyme, even at high concentrations. On the basis of molecular modeling studies, we propose that the GABA-AT active site has an accessory binding pocket that accommodates the vinyl group of vigabatrin and the fluoromethyl group of AFPA, but is too narrow to support the extra width of the distal methyl group in the synthesized analogues. (C) 2012 Elsevier Ltd. All rights reserved.
Biochemistry & Molecular Biology Chemistry Chemistry, Medicinal Chemistry, Organic Life Sciences & Biomedicine Pharmacology & Pharmacy Physical Sciences Science & Technology

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