VWF - Collagen Interactions Studied with Single Molecule Force Spectroscopy

Sandra Posch; Tobias Obser; Maria A. Brehm; Hermann Gruber; Reinhard Schneppenheim; Robert Tampé; Peter Hinterdorfer

doi:10.1016/j.bpj.2013.11.2551

VWF - Collagen Interactions Studied with Single Molecule Force Spectroscopy

Sandra Posch, Tobias Obser, Maria A. Brehm, Hermann Gruber, Reinhard Schneppenheim, Robert Tampé, Peter Hinterdorfer

Department of Applied Experimental Biophysics

Research output: Contribution to journal › Article › peer-review

Abstract

Von Willebrand factor (VWF) is a huge multimeric protein that plays a key role in hemostasis. Sites for collagen binding, an initial event of hemostasis, are located in domains A1 and A3 of VWF. Collagen III is believed to interact with the A3-domain, and collagen VI with the A1-domain. The forces and the dynamics of these interactions were investigated with molecular recognition force spectroscopy (MRFS), using substrates with a dense layer of poly (ethylene glycol) chains and terminal benzaldehyde functions for covalent immobilization of collagen.Von Willebrand factor (VWF) is a huge multimeric protein that plays a key role in hemostasis. Sites for collagen binding, an initial event of hemostasis, are located in domains A1 and A3 of VWF. Collagen III is believed to interact with the A3-domain, and collagen VI with the A1-domain. The forces and the dynamics of these interactions were investigated with molecular recognition force spectroscopy (MRFS), using substrates with a dense layer of poly (ethylene glycol) chains and terminal benzaldehyde functions for covalent immobilization of collagen.

Original language	English
Pages (from-to)	450a
Number of pages	1
Journal	Biophysical Journal
Volume	106
Issue number	2
DOIs	https://doi.org/10.1016/j.bpj.2013.11.2551
Publication status	Published - Jan 2014

Fields of science

103 Physics, Astronomy
106006 Biophysics

JKU Focus areas

Engineering and Natural Sciences (in general)

Access to Document

10.1016/j.bpj.2013.11.2551

Cite this

@article{9ce9308352124640acf5eb282816f0eb,

title = "VWF - Collagen Interactions Studied with Single Molecule Force Spectroscopy",

abstract = "Von Willebrand factor (VWF) is a huge multimeric protein that plays a key role in hemostasis. Sites for collagen binding, an initial event of hemostasis, are located in domains A1 and A3 of VWF. Collagen III is believed to interact with the A3-domain, and collagen VI with the A1-domain. The forces and the dynamics of these interactions were investigated with molecular recognition force spectroscopy (MRFS), using substrates with a dense layer of poly (ethylene glycol) chains and terminal benzaldehyde functions for covalent immobilization of collagen.Von Willebrand factor (VWF) is a huge multimeric protein that plays a key role in hemostasis. Sites for collagen binding, an initial event of hemostasis, are located in domains A1 and A3 of VWF. Collagen III is believed to interact with the A3-domain, and collagen VI with the A1-domain. The forces and the dynamics of these interactions were investigated with molecular recognition force spectroscopy (MRFS), using substrates with a dense layer of poly (ethylene glycol) chains and terminal benzaldehyde functions for covalent immobilization of collagen.",

author = "Sandra Posch and Tobias Obser and Brehm, {Maria A.} and Hermann Gruber and Reinhard Schneppenheim and Robert Tamp{\'e} and Peter Hinterdorfer",

year = "2014",

month = jan,

doi = "10.1016/j.bpj.2013.11.2551",

language = "English",

volume = "106",

pages = "450a",

journal = "Biophysical Journal",

issn = "1542-0086",

publisher = "Elsevier",

number = "2",

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TY - JOUR

T1 - VWF - Collagen Interactions Studied with Single Molecule Force Spectroscopy

AU - Posch, Sandra

AU - Obser, Tobias

AU - Brehm, Maria A.

AU - Gruber, Hermann

AU - Schneppenheim, Reinhard

AU - Tampé, Robert

AU - Hinterdorfer, Peter

PY - 2014/1

Y1 - 2014/1

N2 - Von Willebrand factor (VWF) is a huge multimeric protein that plays a key role in hemostasis. Sites for collagen binding, an initial event of hemostasis, are located in domains A1 and A3 of VWF. Collagen III is believed to interact with the A3-domain, and collagen VI with the A1-domain. The forces and the dynamics of these interactions were investigated with molecular recognition force spectroscopy (MRFS), using substrates with a dense layer of poly (ethylene glycol) chains and terminal benzaldehyde functions for covalent immobilization of collagen.Von Willebrand factor (VWF) is a huge multimeric protein that plays a key role in hemostasis. Sites for collagen binding, an initial event of hemostasis, are located in domains A1 and A3 of VWF. Collagen III is believed to interact with the A3-domain, and collagen VI with the A1-domain. The forces and the dynamics of these interactions were investigated with molecular recognition force spectroscopy (MRFS), using substrates with a dense layer of poly (ethylene glycol) chains and terminal benzaldehyde functions for covalent immobilization of collagen.

AB - Von Willebrand factor (VWF) is a huge multimeric protein that plays a key role in hemostasis. Sites for collagen binding, an initial event of hemostasis, are located in domains A1 and A3 of VWF. Collagen III is believed to interact with the A3-domain, and collagen VI with the A1-domain. The forces and the dynamics of these interactions were investigated with molecular recognition force spectroscopy (MRFS), using substrates with a dense layer of poly (ethylene glycol) chains and terminal benzaldehyde functions for covalent immobilization of collagen.Von Willebrand factor (VWF) is a huge multimeric protein that plays a key role in hemostasis. Sites for collagen binding, an initial event of hemostasis, are located in domains A1 and A3 of VWF. Collagen III is believed to interact with the A3-domain, and collagen VI with the A1-domain. The forces and the dynamics of these interactions were investigated with molecular recognition force spectroscopy (MRFS), using substrates with a dense layer of poly (ethylene glycol) chains and terminal benzaldehyde functions for covalent immobilization of collagen.

U2 - 10.1016/j.bpj.2013.11.2551

DO - 10.1016/j.bpj.2013.11.2551

M3 - Article

SN - 1542-0086

VL - 106

SP - 450a

JO - Biophysical Journal

JF - Biophysical Journal

IS - 2

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