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Farnesylated peptides in model membranes: a biophysical investigation
Umeå University, Faculty of Medicine, Medical Biochemistry and Biophsyics.
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2004 (English)In: European Biophysics Journal, ISSN 0175-7571 (Print) 1432-1017 (Online), Vol. 33, no 4, 300-9 p.Article in journal (Refereed) Published
Abstract [en]

Protein prenylation plays an important role in signal transduction, protein–protein interactions, and the localization and association of proteins with membranes. Using three different techniques, this study physically characterizes the interactions between model dimyristoylphosphatidylcholine membranes and a series of farnesylated peptides. Magic angle spinning nuclear Overhauser enhancement spectroscopy and differential scanning calorimetry reveal that both charged [Ac-Asn-Lys-Asn-Cys-(farnesyl)-OMe and Ac-Asn-Lys-Asn-Cys-(farnesyl)-NH2] and uncharged [Ac-Cys-(farnesyl)-OMe and farnesol] species partition into dimyristoylphosphatidylcholine bilayers. Calorimetry and vesicle fluctuation analysis of giant unilamellar vesicles show that the charged peptides modestly decrease the main gel–fluid phase transition and markedly increase the bending rigidity of large unilamellar vesicles. Uncharged species, on the other hand, dramatically decrease the main phase transition and modestly decrease the bending rigidity. No difference with carboxyl methylation is detected.

Place, publisher, year, edition, pages
2004. Vol. 33, no 4, 300-9 p.
Keyword [en]
Differential scanning calorimetry, Lipid bilayer, MAS-NOESY NMR, Mechanical properties, Vesicle fluctuation analysis
Identifiers
URN: urn:nbn:se:umu:diva-14204DOI: doi:10.1007/s00249-003-0368-xOAI: oai:DiVA.org:umu-14204DiVA: diva2:153875
Available from: 2007-05-24 Created: 2007-05-24 Last updated: 2011-01-12Bibliographically approved

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Sparrman, TobiasLindblom, Göran

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