Secondary structure in de novo designed peptides induced by electrostatic interaction with a lipid bilayer membrane
(2010) In Langmuir 26(9). p.6437-6448- Abstract
- We show that it is possible to induce a defined secondary structure in de novo 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 α-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... (More)
- We show that it is possible to induce a defined secondary structure in de novo 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 α-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 α-helices or β-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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/56978298-b0e5-41e9-9f47-27980e926812
- author
- Nygren, Patrik ; Lundqvist, Martin LU ; Liedberg, Bo ; Jonsson, Bengt-Harald and Ederth, Thomas
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 26
- issue
- 9
- pages
- 12 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:77951680622
- ISSN
- 0743-7463
- DOI
- 10.1021/la100027n
- language
- English
- LU publication?
- no
- id
- 56978298-b0e5-41e9-9f47-27980e926812
- date added to LUP
- 2021-10-19 12:08:42
- date last changed
- 2022-03-11 20:49:07
@article{56978298-b0e5-41e9-9f47-27980e926812,
abstract = {{We show that it is possible to induce a defined secondary structure in de novo 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 α-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 α-helices or β-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.}},
author = {{Nygren, Patrik and Lundqvist, Martin and Liedberg, Bo and Jonsson, Bengt-Harald and Ederth, Thomas}},
issn = {{0743-7463}},
language = {{eng}},
number = {{9}},
pages = {{6437--6448}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Langmuir}},
title = {{Secondary structure in de novo designed peptides induced by electrostatic interaction with a lipid bilayer membrane}},
url = {{http://dx.doi.org/10.1021/la100027n}},
doi = {{10.1021/la100027n}},
volume = {{26}},
year = {{2010}},
}