Single-Molecule Kinetics of Protein Adsorption on Thin Nylon-6,6 Films

Hao Shen; Lawrence J. Tauzin; Wenxiao Wang; Benjamin Hoener; Bo Shuang; Lydia Kisley; Anneli Hoggard; Christy F. Landes

doi:10.1021/acs.analchem.5b04081

Single-Molecule Kinetics of Protein Adsorption on Thin Nylon-6,6 Films

Hao Shen, Lawrence J. Tauzin, Wenxiao Wang, Benjamin Hoener, Bo Shuang, Lydia Kisley, Anneli Hoggard, Christy F. Landes

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

Abstract

Understanding and controlling protein adsorption on surfaces is critical to a range of biological and materials applications. Kinetic details that provide the equilibrium and nonequilibrium mechanisms are difficult to acquire. In this work, single-molecule fluorescence microscopy was used to study the adsorption of Alexa 555 labeled α-lactalbumin (α-LA) on two chemically identical but morphologically different polymer surfaces: flat and porous nylon-6,6 thin films. The adsorption kinetics of spatially resolved single molecule α-LA binding to nylon films were quantified by a monolayer adsorption model. The surface morphology of the porous nylon-6,6 films increased the number of adsorption sites but decreased the binding affinity compared to the flat films. Such single-molecule based kinetic studies may be extended to various protein-polymer interactions.

Original language	English (US)
Pages (from-to)	9926-9933
Number of pages	8
Journal	Analytical Chemistry
Volume	88
Issue number	20
DOIs	https://doi.org/10.1021/acs.analchem.5b04081
State	Published - Oct 18 2016
Externally published	Yes

ASJC Scopus subject areas

Analytical Chemistry

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10.1021/acs.analchem.5b04081

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title = "Single-Molecule Kinetics of Protein Adsorption on Thin Nylon-6,6 Films",

abstract = "Understanding and controlling protein adsorption on surfaces is critical to a range of biological and materials applications. Kinetic details that provide the equilibrium and nonequilibrium mechanisms are difficult to acquire. In this work, single-molecule fluorescence microscopy was used to study the adsorption of Alexa 555 labeled α-lactalbumin (α-LA) on two chemically identical but morphologically different polymer surfaces: flat and porous nylon-6,6 thin films. The adsorption kinetics of spatially resolved single molecule α-LA binding to nylon films were quantified by a monolayer adsorption model. The surface morphology of the porous nylon-6,6 films increased the number of adsorption sites but decreased the binding affinity compared to the flat films. Such single-molecule based kinetic studies may be extended to various protein-polymer interactions.",

author = "Hao Shen and Tauzin, {Lawrence J.} and Wenxiao Wang and Benjamin Hoener and Bo Shuang and Lydia Kisley and Anneli Hoggard and Landes, {Christy F.}",

note = "Funding Information: This research was supported by 3M, the NSF (Grant CHE- 1151647), and the Welch Foundation (Grant C-1787). L.K. acknowledges the NSF for Graduate Research Fellowship 0940902. We thank the Willson research group at University of Houston for providing the protein samples and the Link group at Rice University for discussions. Publisher Copyright: {\textcopyright} 2016 American Chemical Society.",

year = "2016",

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doi = "10.1021/acs.analchem.5b04081",

language = "English (US)",

volume = "88",

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AU - Shen, Hao

AU - Tauzin, Lawrence J.

AU - Wang, Wenxiao

AU - Hoener, Benjamin

AU - Shuang, Bo

AU - Kisley, Lydia

AU - Hoggard, Anneli

AU - Landes, Christy F.

N1 - Funding Information: This research was supported by 3M, the NSF (Grant CHE- 1151647), and the Welch Foundation (Grant C-1787). L.K. acknowledges the NSF for Graduate Research Fellowship 0940902. We thank the Willson research group at University of Houston for providing the protein samples and the Link group at Rice University for discussions. Publisher Copyright: © 2016 American Chemical Society.

PY - 2016/10/18

Y1 - 2016/10/18

N2 - Understanding and controlling protein adsorption on surfaces is critical to a range of biological and materials applications. Kinetic details that provide the equilibrium and nonequilibrium mechanisms are difficult to acquire. In this work, single-molecule fluorescence microscopy was used to study the adsorption of Alexa 555 labeled α-lactalbumin (α-LA) on two chemically identical but morphologically different polymer surfaces: flat and porous nylon-6,6 thin films. The adsorption kinetics of spatially resolved single molecule α-LA binding to nylon films were quantified by a monolayer adsorption model. The surface morphology of the porous nylon-6,6 films increased the number of adsorption sites but decreased the binding affinity compared to the flat films. Such single-molecule based kinetic studies may be extended to various protein-polymer interactions.

AB - Understanding and controlling protein adsorption on surfaces is critical to a range of biological and materials applications. Kinetic details that provide the equilibrium and nonequilibrium mechanisms are difficult to acquire. In this work, single-molecule fluorescence microscopy was used to study the adsorption of Alexa 555 labeled α-lactalbumin (α-LA) on two chemically identical but morphologically different polymer surfaces: flat and porous nylon-6,6 thin films. The adsorption kinetics of spatially resolved single molecule α-LA binding to nylon films were quantified by a monolayer adsorption model. The surface morphology of the porous nylon-6,6 films increased the number of adsorption sites but decreased the binding affinity compared to the flat films. Such single-molecule based kinetic studies may be extended to various protein-polymer interactions.

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Single-Molecule Kinetics of Protein Adsorption on Thin Nylon-6,6 Films

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