PLA2 Interfacial Activation on Lipid Interfaces Promoting Fibril Formation

Code, Christian

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PLA2 Interfacial Activation on Lipid Interfaces Promoting Fibril Formation



Title:	PLA2 Interfacial Activation on Lipid Interfaces Promoting Fibril Formation
Author(s):	Code, Christian
Date:	2013
Language:	en
Pages:	66 + app. 44
Department:	Lääketieteellisen tekniikan ja laskennallisen tieteen laitos Department of Biomedical Engineering and Computational Science
ISBN:	978-952-60-5382-0 (electronic) 978-952-60-5381-3 (printed)
Series:	Aalto University publication series DOCTORAL DISSERTATIONS, 164/2013
ISSN:	1799-4942 (electronic) 1799-4934 (printed) 1799-4934 (ISSN-L)
Supervising professor(s):	Kinnunen, Paavo K. J., Prof., Aalto University, Department of Biomedical Engineering and Computational Science, Finland
Thesis advisor(s):	Kinnunen, Paavo K. J., Prof., Aalto University, Department of Biomedical Engineering and Computational Science, Finland
Subject:	Biotechnology
Keywords:	liposome, PLA2, peptide, phospholipid, amyloid, protein-lipid interaction, dimer, temporin B, heat-shock protein, oxidized phospholipids
	OEVS yes
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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.
Parts: [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. [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. [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. [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.
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