Dynamic footprint of sequestration in the molecular fluctuations of osteopontin.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8042637
- author
- Lenton, S ; Seydel, T ; Nylander, Tommy LU ; Holt, C ; Härtlein, M ; Teixeira, S and Zaccai, G
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of the Royal Society Interface
- volume
- 12
- issue
- 110
- article number
- 20150506
- publisher
- The Royal Society of Canada
- external identifiers
-
- pmid:26354827
- wos:000363224700005
- scopus:84942046000
- pmid:26354827
- 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
- 2016-04-01 09:54:38
- date last changed
- 2022-04-12 00:01:56
@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.}},
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 = {{The Royal Society of Canada}},
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}},
doi = {{10.1098/rsif.2015.0506}},
volume = {{12}},
year = {{2015}},
}