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Secondary Structure in de Novo Designed Peptides Induced by Electrostatic Interaction with a Lipid Bilayer Membrane
Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology, Molecular Biotechnology. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology, Molecular Biotechnology. Linköping University, The Institute of Technology.
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2010 (English)In: LANGMUIR, ISSN 0743-7463, Vol. 26, no 9, 6437-6448 p.Article in journal (Refereed) Published
Abstract [en]

We show that it is possible to induce a defined secondary structure in de nova designed peptides upon electrostatic attachment to negatively charged lipid bilayer vesicles without partitioning of the peptides into the membrane, and that the secondary structure can be varied via small changes in the primary amino acid sequence of the peptides. The peptides have a random-coil conformation in solution, and results from far-UV circular dichroism spectroscopy demonstrate that the structure induced by the interaction with silica nanoparticles is solely alpha-helical and also strongly pH-dependent. The present study shows that negatively charged vesicles, to which the peptides are electrostatically adsorbed via cationic amino acid residues, induce either alpha-helices or beta-sheets and that the conformation is dependent on both lipid composition and variations in peptide primary structure. The pH-dependence of the vesicle-induced peptide secondary structure is weak, which correlates well with small differences in the vesicles electrophoretic mobility, and thus the surface charge, as the pH is varied.

Place, publisher, year, edition, pages
ACS American Chemical Society , 2010. Vol. 26, no 9, 6437-6448 p.
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:liu:diva-56297DOI: 10.1021/la100027nISI: 000276969700056OAI: oai:DiVA.org:liu-56297DiVA: diva2:318310
Note

The previous status of this article was Manuscript.

Available from: 2010-05-07 Created: 2010-05-07 Last updated: 2017-01-11
In thesis
1. Structural and Functional Studies of De Novo Designed Peptides at Surfaces
Open this publication in new window or tab >>Structural and Functional Studies of De Novo Designed Peptides at Surfaces
2008 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The work presented in this thesis deals with the structural and functional properties of peptides at surfaces. The interaction of peptides with surfaces is an ever so common occurrence in our every day life, from the bug squashed on the windshield of our car to the barnacle on our boat, and from the blood plasma used in the hospital to the proteins in our cells. The effect these occurrences has on our lives is diverse, the bug is annoying whereas the barnacle settlement of ship hull is costly for marine transportation, the blood plasma contains components of vital importance for our immunological defense system and the proteins in our cells are crucial for regulatory processes and life.One part of this thesis, performed as a part of the EU-founded project AMBIO, deals with the concept of marine biofouling. A number of short peptides have been designed, synthesized, and used to investigate their effect on the settlement on marine biofoulers, such as the Ulva linza algae and the Navicula diatom, on template surfaces coated with thin layers of these molecules. The surfaces have been thoroughly investigated with respect of their physio-chemical properties before and after submersion in artificial seawater and ultimately in suspensions containing the organisms. The most interesting results were obtained with an arginine-rich peptide coating that when introduced to Ulva linza zoospores, displayed extensive settlement, compared to reference surfaces. In addition, a large fraction of the settled spores had an abnormal morphology.The other part of this thesis is focused on designed peptides that when adsorbed on a negatively charged surface adopts a well-defined secondary structure, either α-helical or β-sheet. Precisely placed amino acids in the peptides will strongly disfavor structure in solution, primarily due to electrostatic repulsion, but when the peptides are adsorbed on the negatively charged surfaces, they adopt a well-defined secondary structure due to ion pair bonding. These interactions have been thoroughly investigated by systematic variations of the side-chains. In order to determine the factors contributing to the induced structure, several peptides with different amino acid sequences have been synthesized. Factors that have been investigated include 1) the positive charge density, 2) distribution of positive charges, 3) negative charge density, 4) increasing hydrophobicity, and 5) incorporating amino acids with different helix propensities. Moreover, pH dependence and the effect of different interaction partners have also been investigated. It has also been shown that the system can be modified to incorporate a catalytic site that is only active when the helix is formed. This research will increase our understanding of peptide-surface interactions and might be of importance for both bionanotechnology and medicine.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2008. 52 p.
Series
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1199
Keyword
Biofouling, vesicles, nanoparticles, peptide, peptide design, circular dichroism
National Category
Physical Chemistry
Identifiers
urn:nbn:se:liu:diva-15022 (URN)978-91-7393-840-2 (ISBN)
Public defence
2008-09-05, Planck, Campus Valla, Linköpings universitet, Linköping, 10:15 (English)
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Available from: 2008-10-09 Created: 2008-10-09 Last updated: 2017-01-11Bibliographically approved

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Nygren, PatrikLundqvist, MartinLiedberg, BoJonsson, Bengt-HaraldEderth, Thomas

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