Fundamental design principles that guide induction of helix upon formation of stable peptide-nanoparticle complexes
(2008) In Nano Letters 8(7). p.1844-1852- Abstract
- We have shown that it is possible to design a peptide that has a very low helical content when free in solution but that adopts a well-defined helix when interacting with silica nanoparticles. From a systematic variation of the amino acid composition and distribution in designed peptides, it has been shown that the ability to form helical structure upon binding to the silica surface is dominated by two factors. First, the helical content is strongly correlated with the net positive charge on the side of the helix that interacts with the silica, and arginine residues are strongly favored over lysine residues in these positions. The second important factor is to have a high net negative charge on the side of the helix that faces the... (More)
- We have shown that it is possible to design a peptide that has a very low helical content when free in solution but that adopts a well-defined helix when interacting with silica nanoparticles. From a systematic variation of the amino acid composition and distribution in designed peptides, it has been shown that the ability to form helical structure upon binding to the silica surface is dominated by two factors. First, the helical content is strongly correlated with the net positive charge on the side of the helix that interacts with the silica, and arginine residues are strongly favored over lysine residues in these positions. The second important factor is to have a high net negative charge on the side of the helix that faces the solution. Apparently, both attractive and repulsive electrostatic forces dominate the induction and stabilization of a bound helix. It is also evident that using amino acids that have high propensity to form helix in solution are also advantageous for the formation of helix on surfaces. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/c66c85b3-2866-4f93-afc9-b8c155f5a085
- author
- Nygren, Patrik ; Lundqvist, Martin LU ; Broo, Klas and Jonsson, Bengt-Harald
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Nano Letters
- volume
- 8
- issue
- 7
- pages
- 9 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:53149113846
- ISSN
- 1530-6992
- DOI
- 10.1021/nl080386s
- language
- English
- LU publication?
- no
- id
- c66c85b3-2866-4f93-afc9-b8c155f5a085
- date added to LUP
- 2021-10-19 12:04:52
- date last changed
- 2022-02-02 00:39:27
@article{c66c85b3-2866-4f93-afc9-b8c155f5a085,
abstract = {{We have shown that it is possible to design a peptide that has a very low helical content when free in solution but that adopts a well-defined helix when interacting with silica nanoparticles. From a systematic variation of the amino acid composition and distribution in designed peptides, it has been shown that the ability to form helical structure upon binding to the silica surface is dominated by two factors. First, the helical content is strongly correlated with the net positive charge on the side of the helix that interacts with the silica, and arginine residues are strongly favored over lysine residues in these positions. The second important factor is to have a high net negative charge on the side of the helix that faces the solution. Apparently, both attractive and repulsive electrostatic forces dominate the induction and stabilization of a bound helix. It is also evident that using amino acids that have high propensity to form helix in solution are also advantageous for the formation of helix on surfaces.}},
author = {{Nygren, Patrik and Lundqvist, Martin and Broo, Klas and Jonsson, Bengt-Harald}},
issn = {{1530-6992}},
language = {{eng}},
number = {{7}},
pages = {{1844--1852}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Nano Letters}},
title = {{Fundamental design principles that guide induction of helix upon formation of stable peptide-nanoparticle complexes}},
url = {{http://dx.doi.org/10.1021/nl080386s}},
doi = {{10.1021/nl080386s}},
volume = {{8}},
year = {{2008}},
}