Single-Molecule Kinetics of Protein Adsorption on Thin Nylon-6,6 Films
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 t...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2016-10, Vol.88 (20), p.9926-9933 |
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| container_title | Analytical chemistry (Washington) |
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| creator | Shen, Hao Tauzin, Lawrence J Wang, Wenxiao Hoener, Benjamin Shuang, Bo Kisley, Lydia Hoggard, Anneli Landes, Christy F |
| description | 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. |
| doi_str_mv | 10.1021/acs.analchem.5b04081 |
| format | Article |
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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. 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Such single-molecule based kinetic studies may be extended to various protein-polymer interactions.</description><subject>Adsorption</subject><subject>Affinity</subject><subject>Binding</subject><subject>Binding sites</subject><subject>Enzyme kinetics</subject><subject>Microscopy</subject><subject>Morphology</subject><subject>Nylons</subject><subject>Protein adsorption</subject><subject>Proteins</subject><subject>Surface chemistry</subject><subject>Thin films</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqNkVtLwzAYhoMobk7_gUjBGy_s_HJOL2U4FecBnNela1MXSZvZtBf792YnBS9ECAQ-nvdN-B6ETjEMMRB8leV-mNWZzee6GvIZMFB4D_UxJxALpcg-6gMAjYkE6KEj7z8AMAYsDlGPSJ4khMo-Gr-a-t3q-NFZnXdWRw-m1q3JfeTK6KVxrTZ1dF141yxa4-oonOk8jJ6W1tWxuBTR2NjKH6ODMrNen2zvAXob30xHd_Hk-fZ-dD2JMyZ5GyuqGBCdSEwpTgB0RhQFRovwR8HEekoTRgqhmJqJolCalglQ4AEqVUEH6GLTu2jcZ6d9m1bG59rarNau8ylWnFPJgIl_oJQzpmQIDND5L_TDdU3Y7ZoiSVitZIFiGypvnPeNLtNFY6qsWaYY0pWSNChJd0rSrZIQO9uWd7NKF9-hnYMAwAZYxX8e_qvzC7xgleQ</recordid><startdate>20161018</startdate><enddate>20161018</enddate><creator>Shen, Hao</creator><creator>Tauzin, Lawrence J</creator><creator>Wang, Wenxiao</creator><creator>Hoener, Benjamin</creator><creator>Shuang, Bo</creator><creator>Kisley, Lydia</creator><creator>Hoggard, Anneli</creator><creator>Landes, Christy F</creator><general>American Chemical Society</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U7</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20161018</creationdate><title>Single-Molecule Kinetics of Protein Adsorption on Thin Nylon-6,6 Films</title><author>Shen, Hao ; 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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.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>27599237</pmid><doi>10.1021/acs.analchem.5b04081</doi><tpages>8</tpages></addata></record> |
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| source | ACS Publications |
| subjects | Adsorption Affinity Binding Binding sites Enzyme kinetics Microscopy Morphology Nylons Protein adsorption Proteins Surface chemistry Thin films |
| title | Single-Molecule Kinetics of Protein Adsorption on Thin Nylon-6,6 Films |
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