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Esben Skipper Sørensen

Adsorption and enzymatic cleavage of osteopontin at interfaces with different surface chemistries

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Adsorption and enzymatic cleavage of osteopontin at interfaces with different surface chemistries. / Malmström, Jenny; Shipovskov, Stepan; Christensen, Brian; Sørensen, Esben Skipper; Kingshott, Peter; Sutherland, Duncan.

In: Biointerphases, Vol. 4, No. 3, 01.09.2009, p. 47-55.

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Malmström, Jenny ; Shipovskov, Stepan ; Christensen, Brian ; Sørensen, Esben Skipper ; Kingshott, Peter ; Sutherland, Duncan. / Adsorption and enzymatic cleavage of osteopontin at interfaces with different surface chemistries. In: Biointerphases. 2009 ; Vol. 4, No. 3. pp. 47-55.

Bibtex

@article{24174f20920611dea092000ea68e967b,
title = "Adsorption and enzymatic cleavage of osteopontin at interfaces with different surface chemistries",
abstract = "Osteopontin is a highly charged glycoprotein present in the extra cellular matrix of a wide range of tissues. It is, in particular, relevant for biomaterials through its role in mineralized tissue remodeling. The adsorption and enzymatic cleavage of osteopontin at four different surface chemistries (methyl-, carboxylic-, and amine-terminated alkanethiol self-assembled monolayers and bare gold) have been studied utilizing a combination of the quartz crystal microbalance with dissipation and surface plasmon resonance. Full length bovine milk osteopontin was used which is well characterized with respect to post-translational modifications. Osteopontin adsorbed at all the surfaces formed thin (approximately 2-5 nm) hydrated layers with the highest amount of protein and the highest density layers observed at the hydrophobic surface. Less protein and a higher level of hydration was observed at the polar surfaces with the highest level of hydration being observed at the gold surface. The energy dissipation of these thin films (as measured by the DeltaD/DeltaF value) was altered at the different surface chemistries and interestingly a higher dissipation correlated with a higher density. Thrombin was able to bind and cleave the surface bound osteopontin at the hydrophobic surface. The altered levels of osteopontin binding, hydration of the layer, and susceptibility to thrombin cleavage suggest that osteopontin adopts different conformations and/or orientations at the different material surfaces.",
author = "Jenny Malmstr{\"o}m and Stepan Shipovskov and Brian Christensen and S{\o}rensen, {Esben Skipper} and Peter Kingshott and Duncan Sutherland",
year = "2009",
month = sep,
day = "1",
doi = "10.1116/1.3187529",
language = "English",
volume = "4",
pages = "47--55",
journal = "Biointerphases",
issn = "1934-8630",
publisher = "AMER INST PHYSICS",
number = "3",

}

RIS

TY - JOUR

T1 - Adsorption and enzymatic cleavage of osteopontin at interfaces with different surface chemistries

AU - Malmström, Jenny

AU - Shipovskov, Stepan

AU - Christensen, Brian

AU - Sørensen, Esben Skipper

AU - Kingshott, Peter

AU - Sutherland, Duncan

PY - 2009/9/1

Y1 - 2009/9/1

N2 - Osteopontin is a highly charged glycoprotein present in the extra cellular matrix of a wide range of tissues. It is, in particular, relevant for biomaterials through its role in mineralized tissue remodeling. The adsorption and enzymatic cleavage of osteopontin at four different surface chemistries (methyl-, carboxylic-, and amine-terminated alkanethiol self-assembled monolayers and bare gold) have been studied utilizing a combination of the quartz crystal microbalance with dissipation and surface plasmon resonance. Full length bovine milk osteopontin was used which is well characterized with respect to post-translational modifications. Osteopontin adsorbed at all the surfaces formed thin (approximately 2-5 nm) hydrated layers with the highest amount of protein and the highest density layers observed at the hydrophobic surface. Less protein and a higher level of hydration was observed at the polar surfaces with the highest level of hydration being observed at the gold surface. The energy dissipation of these thin films (as measured by the DeltaD/DeltaF value) was altered at the different surface chemistries and interestingly a higher dissipation correlated with a higher density. Thrombin was able to bind and cleave the surface bound osteopontin at the hydrophobic surface. The altered levels of osteopontin binding, hydration of the layer, and susceptibility to thrombin cleavage suggest that osteopontin adopts different conformations and/or orientations at the different material surfaces.

AB - Osteopontin is a highly charged glycoprotein present in the extra cellular matrix of a wide range of tissues. It is, in particular, relevant for biomaterials through its role in mineralized tissue remodeling. The adsorption and enzymatic cleavage of osteopontin at four different surface chemistries (methyl-, carboxylic-, and amine-terminated alkanethiol self-assembled monolayers and bare gold) have been studied utilizing a combination of the quartz crystal microbalance with dissipation and surface plasmon resonance. Full length bovine milk osteopontin was used which is well characterized with respect to post-translational modifications. Osteopontin adsorbed at all the surfaces formed thin (approximately 2-5 nm) hydrated layers with the highest amount of protein and the highest density layers observed at the hydrophobic surface. Less protein and a higher level of hydration was observed at the polar surfaces with the highest level of hydration being observed at the gold surface. The energy dissipation of these thin films (as measured by the DeltaD/DeltaF value) was altered at the different surface chemistries and interestingly a higher dissipation correlated with a higher density. Thrombin was able to bind and cleave the surface bound osteopontin at the hydrophobic surface. The altered levels of osteopontin binding, hydration of the layer, and susceptibility to thrombin cleavage suggest that osteopontin adopts different conformations and/or orientations at the different material surfaces.

U2 - 10.1116/1.3187529

DO - 10.1116/1.3187529

M3 - Journal article

C2 - 20408723

VL - 4

SP - 47

EP - 55

JO - Biointerphases

JF - Biointerphases

SN - 1934-8630

IS - 3

ER -