Trends for isolated amino acids and dipeptides: Conformation, divalent ion binding, and remarkable similarity of binding to calcium and lead

dc.contributorAalto-yliopistofi
dc.contributorAalto Universityen
dc.contributor.authorRopo, M.en_US
dc.contributor.authorBlum, Volkeren_US
dc.contributor.authorBaldauf, Carstenen_US
dc.contributor.departmentDepartment of Applied Physicsen
dc.contributor.organizationFritz Haber Institute of the Max Planck Societyen_US
dc.date.accessioned2017-11-21T13:37:45Z
dc.date.available2017-11-21T13:37:45Z
dc.date.issued2016-11-03en_US
dc.description.abstractWe derive structural and binding energy trends for twenty amino acids, their dipeptides, and their interactions with the divalent cations Ca2+, Ba2+, Sr2+, Cd2+, Pb2+, and Hg2+. The underlying data set consists of more than 45,000 first-principles predicted conformers with relative energies up to ∼4 eV (∼400 kJ/mol). We show that only very few distinct backbone structures of isolated amino acids and their dipeptides emerge as lowest-energy conformers. The isolated amino acids predominantly adopt structures that involve an acidic proton shared between the carboxy and amino function. Dipeptides adopt one of two intramolecular-hydrogen bonded conformations C5 or. Upon complexation with a divalent cation, the accessible conformational space shrinks and intramolecular hydrogen bonding is prevented due to strong electrostatic interaction of backbone and side chain functional groups with cations. Clear correlations emerge from the binding energies of the six divalent ions with amino acids and dipeptides. Cd2+ and Hg2+ show the largest binding energies-a potential correlation with their known high acute toxicities. Ca2+ and Pb2+ reveal almost identical binding energies across the entire series of amino acids and dipeptides. This observation validates past indications that ion-mimicry of calcium and lead should play an important role in a toxicological context.en
dc.description.versionPeer revieweden
dc.format.extent1-11
dc.format.mimetypeapplication/pdfen_US
dc.identifier.citationRopo, M, Blum, V & Baldauf, C 2016, ' Trends for isolated amino acids and dipeptides : Conformation, divalent ion binding, and remarkable similarity of binding to calcium and lead ', Scientific Reports, vol. 6, 35772, pp. 1-11 . https://doi.org/10.1038/srep35772en
dc.identifier.doi10.1038/srep35772en_US
dc.identifier.issn2045-2322
dc.identifier.otherPURE UUID: 987b9fe3-f98c-4c1d-8134-cd292270602ben_US
dc.identifier.otherPURE ITEMURL: https://research.aalto.fi/en/publications/987b9fe3-f98c-4c1d-8134-cd292270602ben_US
dc.identifier.otherPURE LINK: http://www.scopus.com/inward/record.url?scp=84994673495&partnerID=8YFLogxKen_US
dc.identifier.otherPURE FILEURL: https://research.aalto.fi/files/16050459/srep35772.pdfen_US
dc.identifier.urihttps://aaltodoc.aalto.fi/handle/123456789/28831
dc.identifier.urnURN:NBN:fi:aalto-201711217652
dc.language.isoenen
dc.relation.ispartofseriesScientific Reportsen
dc.relation.ispartofseriesVolume 6en
dc.rightsopenAccessen
dc.titleTrends for isolated amino acids and dipeptides: Conformation, divalent ion binding, and remarkable similarity of binding to calcium and leaden
dc.typeA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessäfi
dc.type.versionpublishedVersion
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