Submicron streptavidin patterns for protein assembly
| Autor: | Vanessa D. Enriquez-Rios, Sabrina C. Ward, Kimberly L. Turner, Karen L. Christman, Heather D. Maynard, Michael V. Requa, Kenneth A. Bradley |
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| Rok vydání: | 2006 |
| Předmět: |
Streptavidin
Surface Properties Anthrax toxin Methacrylate chemistry.chemical_compound Electrochemistry Fluorescence microscope Organic chemistry Nanotechnology General Materials Science Particle Size Spectroscopy chemistry.chemical_classification Aldehydes Proteins Surfaces and Interfaces Polymer Hydrogen-Ion Concentration Condensed Matter Physics Chemical engineering chemistry Models Chemical Biotinylation Methacrylates Ethylene glycol Protein adsorption |
| Zdroj: | Langmuir : the ACS journal of surfaces and colloids. 22(17) |
| ISSN: | 0743-7463 |
| Popis: | Micron and submicron-scale features of aldehyde functionality were fabricated in polymer films by photolithography to develop a platform for protein immobilization and assembly at a biologically relevant scale. Films containing the pH-reactive polymer poly(3,3'-diethoxypropyl methacrylate) and a photoacid generator (PAG) were patterned from 500 nm to 40 mum by exposure to 365 nm (i-line) light. Upon PAG activation and hydrolysis of acetals, aldehyde groups formed. After the films were incubated with a biotinylated aldehyde reactive probe, the X-ray photoelectron spectroscopy results were consistent with biotin being attached to the surface. The background was subsequently passivated by flood exposure and incubation with an aminooxy-terminated poly(ethylene glycol), resulting in a 98% reduction in nonspecific protein adsorption. Protein patterning and assembly was demonstrated using streptavidin, biotinylated anthrax toxin receptor-1, and the protective antigen moiety of anthrax toxin and confirmed by fluorescence microscopy and atomic force microscopy (AFM). AFM demonstrated that 500 nm protein features were achieved. Because of the abundance of biotinylated proteins, this methodology provides a platform for protein immobilization and assembly for various applications in biotechnology. |
| Databáze: | OpenAIRE |
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