Show simple item record

dc.contributor.authorOwen, Cen_US
dc.contributor.authorJames, Ken_US
dc.contributor.authorSampson, Len_US
dc.contributor.authorAhmed, Sen_US
dc.date.accessioned2018-09-17T15:15:18Z
dc.date.issued2003-01en_US
dc.identifier1en_US
dc.identifier.citationJOURNAL OF PHARMACY AND PHARMACOLOGY, 2003, 55 pp. 85 - 93en_US
dc.identifier.issn0022-3573en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2735
dc.identifier.doi10.1211/002235702568en_US
dc.description.abstractOestrone sulphatase is an important target in the fight against hormone-dependent breast cancer. In an effort to investigate the reported definitive pharmacophore for oestrone sulphatase and continue our search for potent inhibitors of this enzyme, we have undertaken extensive synthesis, biochemical evaluation and physicochemical property determination of a range of benzoic acid based esters. Here, we report the initial results of our study into a series of straight chain alkyl esters of 4-sulphonylbenzoic acid. Using these compounds, we have investigated the involvement of two physicochemical properties, namely logP and pK(a). The results of this study show that there was a strong correlation between the inhibitory activity and the logP of the parent compound. Within the series of compounds studied, hydrophobicity appears to be a more important factor than pK(a) in determining the overall inhibitory activity. In a previous report, we showed that pK(a) plays an important role in stabilizing the phenoxide ion resulting from the hydrolysis of the sulphamate group. Here, we propose that although pK(a) is an important factor in determining the overall inhibitory activity when a wide range of compounds are considered, both hydrophobicity and pK(a) need to be considered in the design of potential inhibitors of oestrone sulphatase.en_US
dc.format.extent85 - 93en_US
dc.languageEnglishen_US
dc.language.isoEnglishen_US
dc.publisherROYAL PHARMACEUTICAL SOC GREAT BRITAINen_US
dc.titleSynthesis and biochemical evaluation of some novel benzoic acid based esters as potential inhibitors of oestrone sulphataseen_US
dc.typeJournal Article
rioxxterms.versionofrecord10.1211/002235702568en_US
rioxxterms.licenseref.startdate2003-01en_US
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfJOURNAL OF PHARMACY AND PHARMACOLOGYen_US
pubs.notesaffiliation: Ahmed, S (Reprint Author), Kingston Univ, Sch Chem & Pharmaceut Sci, Penrhyn Rd, Kingston upon Thames KT1 2EE, Surrey, England. Kingston Univ, Sch Chem & Pharmaceut Sci, Kingston upon Thames KT1 2EE, Surrey, England. Novartis Pharma AG, CH-4002 Basel, Switzerland. Canc Res Inst, Sutton, Surrey, England. keywords-plus: SITE-DIRECTED INHIBITION; ESTRONE SULFATASE; STEROID SULFATASE; AROMATASE INHIBITORS research-areas: Pharmacology & Pharmacy web-of-science-categories: Pharmacology & Pharmacy author-email: [email protected] number-of-cited-references: 15 times-cited: 20 usage-count-last-180-days: 1 usage-count-since-2013: 1 journal-iso: J. Pharm. Pharmacol. doc-delivery-number: 639RX unique-id: ISI:000180644100011 da: 2018-09-17en_US
pubs.notesNot knownen_US
pubs.organisational-group/ICR
pubs.volume55en_US
pubs.embargo.termsNot knownen_US
dc.contributor.icrauthorJames, Karenen_US


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record