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dc.contributor.authorRodríguez, Jéssica
dc.contributor.authorMosquera, Jesús
dc.contributor.authorCouceiro, José R
dc.contributor.authorNitschke, Jonathan R
dc.contributor.authorVázquez, M Eugenio
dc.contributor.authorMascareñas, José L
dc.date.accessioned2017-11-10T17:20:33Z
dc.date.available2017-11-10T17:20:33Z
dc.date.issued2017-01-11
dc.identifier.issn0002-7863
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/268514
dc.description.abstractThe cell internalization of designed oligoarginine peptides equipped with six glutamic acid residues and an anionic pyranine at the N-terminus is triggered upon addition of a supramolecular host. This host binds specifically to the pyranine moiety, enabling the complex to traverse the cell membrane. Interestingly, none of the components, neither the host nor the guest, are able to cross the cell membrane on their own.
dc.format.mediumPrint-Electronic
dc.languageeng
dc.publisherAmerican Chemical Society (ACS)
dc.subjectVero Cells
dc.subjectCell Membrane
dc.subjectAnimals
dc.subjectAnions
dc.subjectMacromolecular Substances
dc.subjectMolecular Structure
dc.subjectChlorocebus aethiops
dc.titleAnion Recognition as a Supramolecular Switch of Cell Internalization.
dc.typeArticle
prism.endingPage58
prism.issueIdentifier1
prism.publicationDate2017
prism.publicationNameJ Am Chem Soc
prism.startingPage55
prism.volume139
dc.identifier.doi10.17863/CAM.14723
dcterms.dateAccepted2016-10-25
rioxxterms.versionofrecord10.1021/jacs.6b11103
rioxxterms.versionAM
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2017-01
dc.contributor.orcidNitschke, Jonathan [0000-0002-4060-5122]
dc.identifier.eissn1520-5126
rioxxterms.typeJournal Article/Review
pubs.funder-project-idEngineering and Physical Sciences Research Council (EP/K039520/1)
cam.issuedOnline2016-12-21
rioxxterms.freetoread.startdate2017-12-16


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