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PLA2 Interfacial Activation on Lipid Interfaces Promoting Fibril Formation

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en
dc.contributor.advisor Kinnunen, Paavo K. J., Prof., Aalto University, Department of Biomedical Engineering and Computational Science, Finland
dc.contributor.author Code, Christian
dc.date.accessioned 2013-11-13T10:00:43Z
dc.date.available 2013-11-13T10:00:43Z
dc.date.issued 2013
dc.identifier.isbn 978-952-60-5382-0 (electronic)
dc.identifier.isbn 978-952-60-5381-3 (printed)
dc.identifier.issn 1799-4942 (electronic)
dc.identifier.issn 1799-4934 (printed)
dc.identifier.issn 1799-4934 (ISSN-L)
dc.identifier.uri https://aaltodoc.aalto.fi/handle/123456789/11342
dc.description.abstract Phospholipase A2 is a widely studied protein found ubiquitously in nature. The protein interacts with the lipid membrane cleaving the phospholipid at the sn-2 position. The interfacial activation mechanism is characterized by a low activity on monomeric substrates but a greatly enhanced activity on aggregated substrates. Several of our papers have elucidated the complex interfacial activation mechanism of this protein from different angles in two very diverse scientific frames: from the view of the lipid and the view of the protein. In this thesis the interfacial activation mechanism of PLA2 is understood to behave in a temporal sequence of events first by binding, dimer formation, oligomer formation and finally by the formation of amyloid-like fibrils. en
dc.format.extent 66 + app. 44
dc.format.mimetype application/pdf
dc.language.iso en en
dc.publisher Aalto University en
dc.publisher Aalto-yliopisto fi
dc.relation.ispartofseries Aalto University publication series DOCTORAL DISSERTATIONS en
dc.relation.ispartofseries 164/2013
dc.relation.haspart [Publication 1]: Code C, Domanov Y, Jutila A, Kinnunen PK. Amyloid-type fiber formation in control of enzyme action: interfacial activation of phospholipase A2. Biophys J. 2008 Jul;95(1):215-24.
dc.relation.haspart [Publication 2]: Code C, Domanov YA, Killian JA, Kinnunen PK. Activation of phospholipase A(2) by temporin B: Formation of antimicrobial peptide-enzyme amyloid-type cofibrils. Biochim Biophys Acta. 2009 May;1788(5):1064-72.
dc.relation.haspart [Publication 3]: Code C, Mahalka AK, Bry K, Kinnunen PK. Activation of phospholipase A2 by 1-palmitoyl-2-(9'-oxo-nonanoyl)-sn-glycero-3-phosphocholine in vitro. Biochim Biophys Acta. 2010 Aug;1798(8):1593-600.
dc.relation.haspart [Publication 4]: Mahalka AK, Code C, Rezaijahromi B, Kirkegaard T, Jäättelä M, Kinnunen PK. Activation of phospholipase A2 by HSP70 in vitro. Biochim Biophys Acta. 2011 Oct;1808 (10): 2569–72.
dc.subject.other Biotechnology en
dc.title PLA2 Interfacial Activation on Lipid Interfaces Promoting Fibril Formation en
dc.type G5 Artikkeliväitöskirja fi
dc.contributor.school Perustieteiden korkeakoulu fi
dc.contributor.school School of Science en
dc.contributor.department Lääketieteellisen tekniikan ja laskennallisen tieteen laitos fi
dc.contributor.department Department of Biomedical Engineering and Computational Science en
dc.subject.keyword liposome en
dc.subject.keyword PLA2 en
dc.subject.keyword peptide en
dc.subject.keyword phospholipid en
dc.subject.keyword amyloid en
dc.subject.keyword protein-lipid interaction en
dc.subject.keyword dimer en
dc.subject.keyword temporin B en
dc.subject.keyword heat-shock protein en
dc.subject.keyword oxidized phospholipids en
dc.identifier.urn URN:ISBN:978-952-60-5382-0
dc.type.dcmitype text en
dc.type.ontasot Doctoral dissertation (article-based) en
dc.type.ontasot Väitöskirja (artikkeli) fi
dc.contributor.supervisor Kinnunen, Paavo K. J., Prof., Aalto University, Department of Biomedical Engineering and Computational Science, Finland
dc.opn Sammalkorpi, Maria, D.Sc. Aalto University, Department of Chemistry, Finland
dc.contributor.lab Helsinki Biophysics and Biomembrane Group en
dc.rev Olkkonen, Vesa, Prof., Minerva Institute for Medical Research, Finland; Mattjus, Peter, Ph.D., Docent, Åbo Akademi University, Finland
dc.date.defence 2013-11-01
local.aalto.digifolder Aalto_64348
local.aalto.digiauth ask

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