Stabilization of Zwitterions in Solution:  GABA Analogues

2005 ◽  
Vol 109 (18) ◽  
pp. 4195-4201 ◽  
Author(s):  
Deborah L. Crittenden ◽  
Mary Chebib ◽  
Meredith J. T. Jordan
Keyword(s):  
Gaba Analogues

Ligand based Drug Design of New Heterocyclic Imines of GABA Analogues: A Molecular Docking Approach for the Discovery of New GABA-AT Inhibitors

2017 ◽  
Vol 17 (1) ◽  
pp. 58-63 ◽  
Author(s):  
Bijo Mathew ◽  
Githa Mathew ◽  
Jerad Suresh ◽  
Dhasthakeer Usman ◽  
Puthucode Subramanyan ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Drug Design ◽  
Docking Approach ◽  
Gaba Analogues

scholarly journals 4-Aminobutyrate (GABA) transporters from the amine-polyamine-choline superfamily: substrate specificity and ligand recognition profile of the 4-aminobutyrate permease from Bacillus subtilis

1998 ◽  
Vol 333 (3) ◽  
pp. 565-571 ◽  
Author(s):  
Casey E. BRECHTEL ◽  
Steven C. KING
Keyword(s):  
Bacillus Subtilis ◽  
Culture Conditions ◽  
Ligand Recognition ◽  
Open Chain ◽  
Conformationally Constrained ◽  
E Coli ◽  
Gaba Transporters ◽  
Transport Defect ◽  
Gaba Analogues ◽  
Limited Culture

A previous study [Ferson, Wray and Fisher (1996) Mol. Microbiol. 22, 693–701] has shown that transposon-mediated disruption of a protein 47% identical to the Escherichia coli GABA (4-aminobutyrate) transporter abolishes the ability of nitrogen-limited culture conditions to induce expression of a GABA transport activity in Bacillus subtilis. Here it is demonstrated directly that the B. subtilis GABA permease (gabP) gene can complement the transport defect in the gabP-negative E. colistrain. Unexpectedly, the ligand-recognition profile of the B. subtilis GabP was found to differ substantially from that of the highly homologous E. coli GabP. Unlike the E. coli GabP, the B. subtilis GabP: (i) exhibits approx. equal preference for the 3-carbon (β-alanine, Km = 9.6 µM) and the 4-carbon (GABA, Km = 37 µM) amino acids, and (ii) resists inhibition by bulky, conformationally constrained compounds (e.g. nipecotic acid, guvacine), which are active against GABA transporters from brain. The present study shows additionally that the B. subtilis GabP can translocate several open-chain GABA analogues (3-aminobutyrate, 3-aminopropanoate, cis-4-aminobutenoate) across the membrane via counterflow against [3H]GABA. Thus, consistent with the idea that the ligand-recognition domain of the B. subtilis GabP is less spacious than that of the close homologue from E. coli, the former exhibits more stringent requirements than the latter for substrate recognition and translocation. These distinct functional characteristics of the E. coli and B. subtilis GABA transporters provide a basis by which to identify ligand-recognition domains within the amine-polyamine-choline transporter superfamily.

A Role of GABA Analogues in the Treatment of Neurological Diseases

2010 ◽  
Vol 17 (22) ◽  
pp. 2338-2347 ◽  
Author(s):  
K. Gajcy ◽  
S. Lochynski ◽  
T. Librowski
Keyword(s):  
Neurological Diseases ◽  
Gaba Analogues

A Novel Gaba Receptor on Central Neurones

1980 ◽  
Vol 25 (4) ◽  
pp. S3-S11 ◽  
Author(s):  
N. G. Bowery ◽  
A. Doble ◽  
D. R. Hill ◽  
A. L. Hudson ◽  
J. Shaw ◽  
...  
Keyword(s):  
Peripheral Nerve ◽  
Ligand Binding ◽  
Gaba Receptor ◽  
Membrane Conductance ◽  
Chloride Ions ◽  
Aminobutyric Acid ◽  
The Novel ◽  
Inhibitory Neurotransmitter ◽  
Gaba Analogues ◽  
Potent Agonist

The features of γ-aminobutyric acid (GABA) as an inhibitory neurotransmitter are described, together with those of its receptor as defined by both iontophoretic and radiolabelled ligand binding techniques. Evidence is presented supporting the existence of a second GABA receptor at both peripheral nerve endings and within the CNS. At the classical receptor, GABA can produce a depolarisation of the ganglion cell body or mediate hyperpolarisation within the CNS by increasing membrane conductance to chloride ions. At this second receptor GABA acts in a bicuculline-insensitive manner to reduce neurotransmitter outflow. Many GABA analogues active at the classical receptor are inactive at the second receptor but by contrast baclofen which is inactive at the classical receptor is a potent agonist at the novel site.

ChemInform Abstract: Synthesis of Sugar-Fused GABA Analogues.

ChemInform ◽  
2010 ◽  
Vol 33 (8) ◽  
pp. no-no
Author(s):  
Frank Schweizer ◽  
Albin Otter ◽  
Ole Hindsgaul
Keyword(s):  
Gaba Analogues

Application of Polymer-Supported Enzymes and Reagents in the Synthesis of γ-Aminobutyric Acid (GABA) Analogues.

ChemInform ◽  
2003 ◽  
Vol 34 (5) ◽  
Author(s):  
Ian R. Baxendale ◽  
Martin Ernst ◽  
Wolf-Ruediger Krahnert ◽  
Steven V. Ley
Keyword(s):  
Aminobutyric Acid ◽  
Gaba Analogues ◽  
Polymer Supported

Enantiomers of cis-constrained and flexible 2-substituted GABA analogues exert opposite effects at recombinant GABAC receptors

2006 ◽  
Vol 14 (2) ◽  
pp. 447-455 ◽  
Author(s):  
Deborah L. Crittenden ◽  
Anna Park ◽  
Jian Qiu ◽  
Richard B. Silverman ◽  
Rujee K. Duke ◽  
...  
Keyword(s):  
Gaba Analogues ◽  
Gabac Receptors
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