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Dynamic footprint of sequestration in the molecular fluctuations of osteopontin.

Lenton, S; Seydel, T; Nylander, Tommy LU ; Holt, C; Härtlein, M; Teixeira, S and Zaccai, G (2015) In Journal of the Royal Society Interface 12(110).
Abstract
The sequestration of calcium phosphate by unfolded proteins is fundamental to the stabilization of biofluids supersaturated with respect to hydroxyapatite, such as milk, blood or urine. The unfolded state of osteopontin (OPN) is thought to be a prerequisite for this activity, which leads to the formation of core-shell calcium phosphate nanoclusters. We report on the structures and dynamics of a native OPN peptide from bovine milk, studied by neutron spectroscopy and small-angle X-ray and neutron scattering. The effects of sequestration are quantified on the nanosecond- ångström resolution by elastic incoherent neutron scattering. The molecular fluctuations of the free phosphopeptide are in agreement with a highly flexible protein. An... (More)
The sequestration of calcium phosphate by unfolded proteins is fundamental to the stabilization of biofluids supersaturated with respect to hydroxyapatite, such as milk, blood or urine. The unfolded state of osteopontin (OPN) is thought to be a prerequisite for this activity, which leads to the formation of core-shell calcium phosphate nanoclusters. We report on the structures and dynamics of a native OPN peptide from bovine milk, studied by neutron spectroscopy and small-angle X-ray and neutron scattering. The effects of sequestration are quantified on the nanosecond- ångström resolution by elastic incoherent neutron scattering. The molecular fluctuations of the free phosphopeptide are in agreement with a highly flexible protein. An increased resilience to diffusive motions of OPN is corroborated by molecular fluctuations similar to those observed for globular proteins, yet retaining conformational flexibilities. The results bring insight into the modulation of the activity of OPN and phosphopeptides with a role in the control of biomineralization. The quantification of such effects provides an important handle for the future design of new peptides based on the dynamics-activity relationship. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of the Royal Society Interface
volume
12
issue
110
publisher
Royal Society
external identifiers
  • pmid:26354827
  • wos:000363224700005
  • scopus:84942046000
ISSN
1742-5662
DOI
10.1098/rsif.2015.0506
language
English
LU publication?
yes
id
1f89af84-86d6-4f6a-8fd3-f6186260a5c6 (old id 8042637)
date added to LUP
2015-10-30 13:08:19
date last changed
2017-07-30 03:02:37
@article{1f89af84-86d6-4f6a-8fd3-f6186260a5c6,
  abstract     = {The sequestration of calcium phosphate by unfolded proteins is fundamental to the stabilization of biofluids supersaturated with respect to hydroxyapatite, such as milk, blood or urine. The unfolded state of osteopontin (OPN) is thought to be a prerequisite for this activity, which leads to the formation of core-shell calcium phosphate nanoclusters. We report on the structures and dynamics of a native OPN peptide from bovine milk, studied by neutron spectroscopy and small-angle X-ray and neutron scattering. The effects of sequestration are quantified on the nanosecond- ångström resolution by elastic incoherent neutron scattering. The molecular fluctuations of the free phosphopeptide are in agreement with a highly flexible protein. An increased resilience to diffusive motions of OPN is corroborated by molecular fluctuations similar to those observed for globular proteins, yet retaining conformational flexibilities. The results bring insight into the modulation of the activity of OPN and phosphopeptides with a role in the control of biomineralization. The quantification of such effects provides an important handle for the future design of new peptides based on the dynamics-activity relationship.},
  articleno    = {20150506},
  author       = {Lenton, S and Seydel, T and Nylander, Tommy and Holt, C and Härtlein, M and Teixeira, S and Zaccai, G},
  issn         = {1742-5662},
  language     = {eng},
  number       = {110},
  publisher    = {Royal Society},
  series       = {Journal of the Royal Society Interface},
  title        = {Dynamic footprint of sequestration in the molecular fluctuations of osteopontin.},
  url          = {http://dx.doi.org/10.1098/rsif.2015.0506},
  volume       = {12},
  year         = {2015},
}