Surfaces for Competitive Selective Bacterial Capture from Protein Solutions

Fang, B. and Gon, S. and Nusslein, K. and Santore, M. M.. (2015) Surfaces for Competitive Selective Bacterial Capture from Protein Solutions. Acs Applied Materials & Interfaces, 7 (19). pp. 10275-10282.

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Active surfaces that form the basis for bacterial sensors for threat detection, food safety, or certain diagnostic applications rely on bacterial adhesion. However, bacteria capture from complex fluids on the active surfaces can be reduced by the competing adsorption of proteins and other large molecules. Such adsorption can also interfere with device performance. As a result, multiple upstream processing steps are frequently employed to separate macromolecules from any cells, which remain in the buffer. Here, we present an economical approach to capture bacteria, without competitive adsorption by proteins, on engineered surfaces that do not employ biomolecular recognition, antibodies, or other molecules with engineered sequences. The surfaces are based on polyethylene glycol (PEG) brushes that, on their own, repel both proteins and bacteria. These PEG brushes backfill the surface around sparsely adsorbed cationic polymer coils (here, poly-r.-lysine (PLL)). The PLL coils are effectively embedded within the brush and produce locally cationic nanoscale regions that attract negatively charged regions of proteins or cells against the steric background repulsion from the PEG brush. By carefully designing the surfaces to include just enough PLL to capture bacteria, but not enough to capture proteins, we achieve sharp selectivity where S. aureus is captured from albumin- or fibrinogen-containing solutions, but free albumin or fibrinogen molecules are rejected from the surface. Bacterial adhesion on these surfaces is not reduced by competitive protein adsorption, in contrast to performance of more uniformly cationic surfaces. Also, protein adsorption to the bacteria does not interfere with capture, at least for the case of S. aureus, to which fibrinogen binds through a specific receptor.

Item Type: Article
Additional Information: ISI Document Delivery No.: CI8XMTimes Cited: 0Cited Reference Count: 47Fang, Bing Gon, Saugata Nuesslein, Klaus Santore, Maria M.Nsf 1025020, 1264855This work was supported by NSF 1025020 and NSF 1264855.Amer chemical socWashington
Uncontrolled Keywords: porous-media
Collections: Nanomanufacturing Research Collection > Nanomanufacturing Nanoscale Science and Engineering Centers > Center for Hierarchical Manufacturing
Depositing User: Robert Stevens
Date Deposited: 12 Nov 2015 18:38
Last Modified: 12 Nov 2015 18:38

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