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dc.contributor.authorPinotsi, Dorothea
dc.contributor.authorGrisanti, Luca
dc.contributor.authorMahou, Pierre
dc.contributor.authorGebauer, Ralph
dc.contributor.authorKaminski, Clemens F
dc.contributor.authorHassanali, Ali
dc.contributor.authorKaminski Schierle, Gabriele S
dc.date.accessioned2016-02-03T16:50:07Z
dc.date.available2016-02-03T16:50:07Z
dc.date.issued2016-03-09
dc.identifier.citationPinotsi et al. Journal of the American Chemical Society (2016), 138(9), pp. 3046–3057. doi: 10.1021/jacs.5b11012
dc.identifier.issn0002-7863
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/253632
dc.description.abstractProtein structures which form fibrils have recently been shown to absorb light at energies in the near UV range and to exhibit a structure-specific fluorescence in the visible range even in the absence of aromatic amino acids. However, the molecular origin of this phenomenon has so far remained elusive. Here, we combine ab initio molecular dynamics simulations and fluorescence spectroscopy to demonstrate that these intrinsically fluorescent protein fibrils are permissive to proton transfer across hydrogen bonds which can lower electron excitation energies and thereby decrease the likelihood of energy dissipation associated with conventional hydrogen bonds. The importance of proton transfer on the intrinsic fluorescence observed in protein fibrils is signified by large reductions in the fluorescence intensity upon either fully protonating, or deprotonating, the fibrils at pH = 0 or 14, respectively. Thus, our results point to the existence of a structure-specific fluorophore that does not require the presence of aromatic residues or multiple bond conjugation that characterize conventional fluorescent systems. The phenomenon may have a wide range of implications in biological systems and in the design of self-assembled functional materials.
dc.description.sponsorshipWe thank Prof. M. Sauer for useful discussions. This work was funded by grants from the Medical Research Council UK (MR/K015850/1 and MR/K02292X/1), Alzheimer Research UK (ARUKEG2012A-1), U.K. EPSRC (EP/H018301/1) and the Wellcome Trust (089703/Z/09/Z). D.P. wishes to acknowledge support from the Swiss National Science Foundation and the Wellcome Trust through personal fellowships. We thank LMB Visual Aids for graphics support.
dc.languageEnglish
dc.language.isoen
dc.publisherAmerican Chemical Society (ACS)
dc.titleProton Transfer and Structure-Specific Fluorescence in Hydrogen Bond-Rich Protein Structures.
dc.typeArticle
dc.provenanceOA-6904
dc.description.versionThis is the author accepted manuscript. The final version is available from the American Chemical Society via http://dx.doi.org/10.1021/jacs.5b11012
prism.endingPage3057
prism.publicationDate2016
prism.publicationNameJ Am Chem Soc
prism.startingPage3046
prism.volume138
dc.rioxxterms.funderMRC
dc.rioxxterms.funderEPSRC
dc.rioxxterms.funderWellcome Trust
dc.rioxxterms.projectidMR/K015850/1
dc.rioxxterms.projectidMR/K02292X/1
dc.rioxxterms.projectidEP/H018301/1
dc.rioxxterms.projectid089703/Z/09/Z
rioxxterms.versionofrecord10.1021/jacs.5b11012
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2016-01-29
dc.contributor.orcidKaminski, Clemens [0000-0002-5194-0962]
dc.contributor.orcidKaminski Schierle, Gabriele [0000-0002-1843-2202]
dc.identifier.eissn1520-5126
rioxxterms.typeJournal Article/Review
pubs.funder-project-idWellcome Trust (089703/Z/09/Z)
pubs.funder-project-idMedical Research Council (MR/K015850/1)
pubs.funder-project-idEngineering and Physical Sciences Research Council (EP/H018301/1)
pubs.funder-project-idMedical Research Council (MC_G1000734)
pubs.funder-project-idMedical Research Council (MR/K02292X/1)
pubs.funder-project-idMedical Research Council (MR/N012453/1)
cam.issuedOnline2016-02-25
rioxxterms.freetoread.startdate2017-01-29


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