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Strings and stripes formed by a protein system interacting via a single-patch attraction

Li, Weimin LU ; Morin, Maxim LU ; Gustafsson, Emil ; Persson, Björn A. LU ; Lund, Mikael LU orcid and Zackrisson Oskolkova, Malin LU (2016) In Soft Matter 12(46). p.9330-9333
Abstract

The phase behavior of lactoferrin has been studied as a function of concentration at a pH and ionic strength where lactoferrin is known to interact effectively via a patch-patch attraction. In contrast to isotropic attractive potentials, the directional attraction gives rise to a different phase or solution behavior. At low concentrations, the protein dimerizes. As the concentration is increased, the protein self-assembles into elongated, stripe-like structures at intermediate protein concentrations, a behavior which has been predicted for the case of attractive one-patch colloids. The stripe phase is surprisingly difficult to detect using conventional techniques, i.e. small-angle X-ray scattering, since only a small fraction of the... (More)

The phase behavior of lactoferrin has been studied as a function of concentration at a pH and ionic strength where lactoferrin is known to interact effectively via a patch-patch attraction. In contrast to isotropic attractive potentials, the directional attraction gives rise to a different phase or solution behavior. At low concentrations, the protein dimerizes. As the concentration is increased, the protein self-assembles into elongated, stripe-like structures at intermediate protein concentrations, a behavior which has been predicted for the case of attractive one-patch colloids. The stripe phase is surprisingly difficult to detect using conventional techniques, i.e. small-angle X-ray scattering, since only a small fraction of the proteins participate in the stripes combined with sedimentation due to micron-sized entities. This is circumvented by monitoring the change in the overall protein concentration by static light scattering and the stripe formation can be followed. For visualization of the structures cryo-TEM is used.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Soft Matter
volume
12
issue
46
pages
4 pages
publisher
Royal Society of Chemistry
external identifiers
  • scopus:84997832006
  • pmid:27819378
  • wos:000389322800008
ISSN
1744-683X
DOI
10.1039/c6sm01841f
language
English
LU publication?
yes
id
39aadfaf-9013-43fd-a1ea-fb39efbb14f7
date added to LUP
2017-04-21 14:02:49
date last changed
2024-01-13 19:23:18
@article{39aadfaf-9013-43fd-a1ea-fb39efbb14f7,
  abstract     = {{<p>The phase behavior of lactoferrin has been studied as a function of concentration at a pH and ionic strength where lactoferrin is known to interact effectively via a patch-patch attraction. In contrast to isotropic attractive potentials, the directional attraction gives rise to a different phase or solution behavior. At low concentrations, the protein dimerizes. As the concentration is increased, the protein self-assembles into elongated, stripe-like structures at intermediate protein concentrations, a behavior which has been predicted for the case of attractive one-patch colloids. The stripe phase is surprisingly difficult to detect using conventional techniques, i.e. small-angle X-ray scattering, since only a small fraction of the proteins participate in the stripes combined with sedimentation due to micron-sized entities. This is circumvented by monitoring the change in the overall protein concentration by static light scattering and the stripe formation can be followed. For visualization of the structures cryo-TEM is used.</p>}},
  author       = {{Li, Weimin and Morin, Maxim and Gustafsson, Emil and Persson, Björn A. and Lund, Mikael and Zackrisson Oskolkova, Malin}},
  issn         = {{1744-683X}},
  language     = {{eng}},
  number       = {{46}},
  pages        = {{9330--9333}},
  publisher    = {{Royal Society of Chemistry}},
  series       = {{Soft Matter}},
  title        = {{Strings and stripes formed by a protein system interacting via a single-patch attraction}},
  url          = {{http://dx.doi.org/10.1039/c6sm01841f}},
  doi          = {{10.1039/c6sm01841f}},
  volume       = {{12}},
  year         = {{2016}},
}