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Determination of Binding Kinetics of Intrinsically Disordered Proteins by Surface Plasmon Resonance

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@article{32d43081264d45d79865cc13649231a5,
title = "Determination of Binding Kinetics of Intrinsically Disordered Proteins by Surface Plasmon Resonance",
abstract = "Surface plasmon resonance (SPR) is an important and convenient method for measuring kinetic rate constants of given molecular interactions, equilibrium binding constants at steady state, or determinations of binding stoichiometry. In its traditional setup, SPR requires that one binding partner is tightly immobilized on the surface of a sensor chip either by direct chemical coupling to the surface-coated carboxymethylated dextran matrix or by non-covalent capture to a high-affinity binding partner that is covalently linked to the surface. The latter design of the sensor surface is highly advantageous compared to the direct chemical coupling as this setup ensures a homogeneous and specific orientation of the immobilized binding partner. This chapter provides guidelines for the design of capturing systems that generally provide high-end kinetic data suitable for determination of binding rate constants. This principle will be illustrated by the binding of synthetic peptides derived from an intrinsically disordered region of the endothelial glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 (GPIHBP1) to captured monoclonal antibodies.",
author = "Leth, {Julie M} and Michael Ploug",
year = "2020",
doi = "10.1007/978-1-0716-0524-0_31",
language = "English",
volume = "2141",
pages = "611--627",
journal = "Methods in Molecular Biology",
issn = "1064-3745",
publisher = "Humana Press, Inc",

}

RIS

TY - JOUR

T1 - Determination of Binding Kinetics of Intrinsically Disordered Proteins by Surface Plasmon Resonance

AU - Leth, Julie M

AU - Ploug, Michael

PY - 2020

Y1 - 2020

N2 - Surface plasmon resonance (SPR) is an important and convenient method for measuring kinetic rate constants of given molecular interactions, equilibrium binding constants at steady state, or determinations of binding stoichiometry. In its traditional setup, SPR requires that one binding partner is tightly immobilized on the surface of a sensor chip either by direct chemical coupling to the surface-coated carboxymethylated dextran matrix or by non-covalent capture to a high-affinity binding partner that is covalently linked to the surface. The latter design of the sensor surface is highly advantageous compared to the direct chemical coupling as this setup ensures a homogeneous and specific orientation of the immobilized binding partner. This chapter provides guidelines for the design of capturing systems that generally provide high-end kinetic data suitable for determination of binding rate constants. This principle will be illustrated by the binding of synthetic peptides derived from an intrinsically disordered region of the endothelial glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 (GPIHBP1) to captured monoclonal antibodies.

AB - Surface plasmon resonance (SPR) is an important and convenient method for measuring kinetic rate constants of given molecular interactions, equilibrium binding constants at steady state, or determinations of binding stoichiometry. In its traditional setup, SPR requires that one binding partner is tightly immobilized on the surface of a sensor chip either by direct chemical coupling to the surface-coated carboxymethylated dextran matrix or by non-covalent capture to a high-affinity binding partner that is covalently linked to the surface. The latter design of the sensor surface is highly advantageous compared to the direct chemical coupling as this setup ensures a homogeneous and specific orientation of the immobilized binding partner. This chapter provides guidelines for the design of capturing systems that generally provide high-end kinetic data suitable for determination of binding rate constants. This principle will be illustrated by the binding of synthetic peptides derived from an intrinsically disordered region of the endothelial glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 (GPIHBP1) to captured monoclonal antibodies.

U2 - 10.1007/978-1-0716-0524-0_31

DO - 10.1007/978-1-0716-0524-0_31

M3 - Journal article

VL - 2141

SP - 611

EP - 627

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

SN - 1064-3745

ER -

ID: 60627027