Farnesylated peptides in model membranes: a biophysical investigation.
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)-NH(2)] 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.
Rowat
Amy C
AC
MEMPHYS Centre for Biomembrane Physics, Department of Physics & Chemistry, University of Southern Denmark, Odense, Denmark.
Brask
Jesper
J
Sparrman
Tobias
T
Jensen
Knud J
KJ
Lindblom
Göran
G
Ipsen
John H
JH
D001703:Biophysics / Q000379:methods; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry*; D004548:Elasticity; D046911:Macromolecular Substances / Q000737:chemistry; D008560:Membrane Fluidity; D008563:Membrane Lipids / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008567:Membranes, Artificial; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D017368:Protein Prenylation; D055672:Static Electricity
D046911:Macromolecular Substances; D008563:Membrane Lipids; D008565:Membrane Proteins; D008567:Membranes, Artificial; D010455:Peptides; D004134:Dimyristoylphosphatidylcholine