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6 results on '"Stephen P. East"'

1. Peptidomimetic inhibitors of bacterial peptide deformylase

Author

Wayne Thomas, Ian Toogood-Johnson, Stephen P. East, Andrew Paul Ayscough, and Steven S. Taylor

Subjects
Peptidomimetic, Clinical Biochemistry, Pharmaceutical Science, Microbial Sensitivity Tests, medicine.disease_cause, Biochemistry, Haemophilus influenzae, Amidohydrolases, Peptide deformylase, chemistry.chemical_compound, Inhibitory Concentration 50, Structure-Activity Relationship, Drug Discovery, medicine, Moiety, Amines, Molecular Biology, Antibacterial agent, Aza Compounds, Hydroxamic acid, Organic Chemistry, Biological activity, Anti-Bacterial Agents, chemistry, Cyclization, Molecular Medicine, Peptidomimetics, Antibacterial activity
Abstract

A series of N-formyl hydroxylamine peptide deformylase inhibitors containing a cyclic azaamino acid moiety between the P1' and P3' substituents are presented. Selected compounds display antibacterial activity against pathogens associated with respiratory tract infections with representative compounds showing excellent MICs against Haemophilus influenzae.

Published
2011

2. An orally bioavailable positive allosteric modulator of the mGlu4 receptor with efficacy in an animal model of motor dysfunction

Author

Adrian Kotei Kotey, Stephen P. East, Kai Gerlach, Mildred Williams, Samantha Jayne Bamford, Adam Flegg, Pui Loke, Mark Whittaker, Ralf Heilker, Gerhard Schänzle, Christian Eickmeier, Mark J. Gemkow, Schubert Hans-Dieter, Matthias G. A. Dietz, Bastian Hengerer, Boris Ferger, John D. Scott, and Przemyslaw Zawadzki

Subjects
medicine.medical_specialty, Allosteric modulator, Clinical Biochemistry, Allosteric regulation, Pharmaceutical Science, Administration, Oral, Catalepsy, Motor Activity, Receptors, Metabotropic Glutamate, Biochemistry, Styrenes, Rats, Sprague-Dawley, Structure-Activity Relationship, Allosteric Regulation, Oral administration, Internal medicine, Drug Discovery, medicine, Structure–activity relationship, Animals, Humans, Receptor, Molecular Biology, Chemistry, Organic Chemistry, Glutamate receptor, medicine.disease, High-Throughput Screening Assays, Rats, Metabotropic receptor, Endocrinology, Pyrimidines, Models, Animal, Molecular Medicine
Abstract

A high-throughput screening campaign identified 4-((E)-styryl)-pyrimidin-2-ylamine (11) as a positive allosteric modulator of the metabotropic glutamate (mGlu) receptor subtype 4. An evaluation of the structure-activity relationships (SAR) of 11 is described and the efficacy of this compound in a haloperidol-induced catalepsy rat model following oral administration is presented.

Published
2010

3. Antibacterial alkoxybenzamide inhibitors of the essential bacterial cell division protein FtsZ

Author

Ian Collins, Mark Whittaker, Caterina Noula, Mihaly Gardiner, Rebecca Ure, David Brown, E.Andrew Boyd, Lloyd George Czaplewski, Rowena Fletcher, Clare Jones, David J. Haydon, Chris Rockley, Valerie Rose, Neil R. Stokes, Stephen P. East, Helena Thomaides-Brears, Peter Ingram, Vincent Henstock, and Leanne Kennison

Subjects
biology, Chemistry, Staphylococcus, Organic Chemistry, Clinical Biochemistry, Pharmaceutical Science, Microbial Sensitivity Tests, Biochemistry, Bacterial cell structure, Anti-Bacterial Agents, Cytoskeletal Proteins, Structure-Activity Relationship, Bacterial Proteins, 3-methoxybenzamide, Drug Discovery, Benzamides, biology.protein, Molecular Medicine, Structure–activity relationship, FtsZ, Molecular Biology
Abstract

3-Methoxybenzamide is a weak inhibitor of the essential bacterial cell division protein FtsZ. Exploration of the structure-activity relationships of 3-methoxybenzamide analogues led to the identification of potent anti-staphylococcal compounds.

Published
2008

4. Arylsulfonamide CB2 receptor agonists: SAR and optimization of CB2 selectivity

Author

Jenkins James Edward, Andreas Ebneth, Doris Riether, Andreas F. Kahrs, Sabine Löbbe, Innocent Mushi, Taylor Malcolm, Kathy O’Shea, Daw-Tsun Shih, Edward Walker, Brian W. Dymock, Monika Ermann, Mark L. Brewer, David S. Thomson, Stephen P. East, Beatriz Noya-Marino, Mark J. Gemkow, and Patricia Amouzegh

Subjects
Agonist, Cannabinoid receptor, Molecular Structure, Stereochemistry, Chemistry, medicine.drug_class, medicine.medical_treatment, High-throughput screening, Organic Chemistry, Clinical Biochemistry, Pharmaceutical Science, Carboxamide, Biochemistry, Receptor, Cannabinoid, CB2, Structure-Activity Relationship, Receptor, Cannabinoid, CB1, Drug Discovery, medicine, Cannabinoid receptor type 2, Molecular Medicine, Structure–activity relationship, lipids (amino acids, peptides, and proteins), Cannabinoid, Receptor, Molecular Biology
Abstract

A high-throughput screening campaign resulted in the discovery of a highly potent dual cannabinoid receptor 1 (CB1) and 2 (CB2) agonist. Following a thorough SAR exploration, a series of selective CB2 full agonists were identified.

Published
2007

5. Design and synthesis of substituted pyridine derivatives as HIF-1alpha prolyl hydroxylase inhibitors

Author

Richard Masaru Kawamoto, Artem G. Evdokimov, Stephen P. East, Justin Sheville, Songtao Zhou, Namal Chithranga Warshakoon, Sean Michael Renock, R.L. Walter, Shengde Wu, Kevin Xu, Angelique Sun Boyer, Matthew Pokross, Marlene Mekel, and Ritu Tiku Bhatt

Subjects
Stereochemistry, medicine.drug_class, Pyridines, Carboxylic acid, Clinical Biochemistry, Procollagen-Proline Dioxygenase, Pharmaceutical Science, Carboxamide, Pyrazole, Biochemistry, Chemical synthesis, Hypoxia-Inducible Factor-Proline Dioxygenases, chemistry.chemical_compound, Prolyl-Hydroxylase Inhibitors, Drug Discovery, Pyridine, medicine, Humans, Molecular Biology, chemistry.chemical_classification, Aryl, Organic Chemistry, chemistry, Drug Design, Molecular Medicine, Procollagen-proline dioxygenase
Abstract

Structure-guided de novo drug design led to the identification of a novel series of substituted pyridine derivatives as HIF-1alpha prolyl hydroxylase inhibitors. Pyridine carboxyamide derivatives bearing a substituted aryl group at the 5-position of the pyridine ring show appreciable activity, while constraining the side chain by placing a pyrazole carboxylic acid generated a potent lead series with consistent activity against EGLN-1.

Published
2006

6. Structure-activity relationships of the peptide deformylase inhibitor BB-3497: modification of the metal binding group

Author

Stephen P. East, Richard S. Todd, Mark Whittaker, Zoë M. Spavold, Smith Helen Katherine, Lisa M. Pratt, Sheila Doel, Steven B. Launchbury, Paul Beckett, Wayne Thomas, and John M. Clements

Subjects
Stereochemistry, medicine.drug_class, Clinical Biochemistry, Pharmaceutical Science, Carboxamide, Microbial Sensitivity Tests, Hydroxamic Acids, Biochemistry, Aminopeptidases, Amidohydrolases, Peptide deformylase, chemistry.chemical_compound, Inhibitory Concentration 50, Structure-Activity Relationship, Hydroxylamine, Formylmethionine deformylase, Drug Discovery, medicine, Enzyme Inhibitors, Molecular Biology, Antibacterial agent, Hydroxamic acid, Binding Sites, biology, Bacteria, Chemistry, Escherichia coli Proteins, Organic Chemistry, Enzyme inhibitor, Metals, biology.protein, Molecular Medicine, Antibacterial activity
Abstract

A series of analogues of the potent peptide deformylase (PDF) inhibitor BB-3497 containing alternative metal binding groups was synthesised. Enzyme inhibition and antibacterial activity data for these compounds revealed that the bidentate hydroxamic acid and N-formyl hydroxylamine structural motifs represent the optimum chelating groups on the pseudopeptidic BB-3497 backbone.

Published
2002

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