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dc.contributor.authorDemuth, Caspar-
dc.contributor.authorZerbe, Oliver-
dc.contributor.authorRognan, Didier-
dc.contributor.authorSöll, Richard-
dc.contributor.authorBeck-Sickinger, Annette-
dc.contributor.authorFolkers, Gerd-
dc.contributor.authorSpichiger, Ursula E.-
dc.date.accessioned2019-01-23T11:21:40Z-
dc.date.available2019-01-23T11:21:40Z-
dc.date.issued2001-
dc.identifier.issn0956-5663de_CH
dc.identifier.issn1873-4235de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/14536-
dc.description.abstractOligopeptides that interact with oxoanions were developed by rational design methods. The substrate-binding site of the enzyme purine nucleoside phosphorylase served as a model for the design of the ionophores. The amino acids involved in the complexation of oxoanions were linked through flexible spacer residues. These spacers were chosen such that the relative orientation of the interacting amino acids was conserved. Several peptide sequences were preselected based on intermolecular H-bond frequencies. These frequencies were calculated from molecular dynamics trajectories of the corresponding peptide-anion complexes and used to score the binding properties of the peptides. The most promising peptides were prepared using solid phase peptide synthesis. Anion binding of the peptide ionophores was screened using circular dichroism (CD) and confirmed by NMR spectroscopy. CD measurements performed in methanol revealed a significant conformational change of a linear undecapeptide upon binding to sulphate ions. Two-dimensional-NMR experiments confirmed that a conformation with high helical content is formed in the presence of sulphate ions. These conformational changes induced by the anion stimulate the development of new transduction mechanisms in chemical sensors.de_CH
dc.language.isoende_CH
dc.publisherElsevierde_CH
dc.relation.ispartofBiosensors and Bioelectronicsde_CH
dc.rightsLicence according to publishing contractde_CH
dc.subject.ddc540: Chemiede_CH
dc.titleA rationally designed oligopeptide shows significant conformational changes upon binding to sulphate ionsde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Chemie und Biotechnologie (ICBT)de_CH
dc.identifier.doi10.1016/S0956-5663(01)00221-4de_CH
zhaw.funding.euNode_CH
zhaw.issue9-12de_CH
zhaw.originated.zhawNode_CH
zhaw.pages.end789de_CH
zhaw.pages.start783de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume16de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
Appears in collections:Publikationen Life Sciences und Facility Management

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