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Title: Bifunctional polyacrylamide based polymers for the specific binding of hexahistidine tagged proteins on gold surfaces

Abstract

We describe a modified bifunctional analogue of polyacrylamide that spontaneously forms self-assembled polymeric thin films on Au surfaces. The film is engineered to specifically bind histidine tagged proteins (6His), while simultaneously remaining inherently resistant to the non-specific adsorption of proteins in solution. The backbone of a polyacrylamide-co-n-acryloxysuccinimide copolymer is functionalized via tandem active ester (NHS) couplings with 3-(methylthio)propylamine (MTP) and nitrilotriacetic acid (NTA). The resulting functionalized polymers form stable and exceptionally hydrophilic thin films that are ~2–5 nm thick, a mass coverage that varies with the MTP graft density. These films are characterized using a variety of techniques (X-ray photoelectron spectroscopy (XPS), reflection absorption infrared spectroscopy (RAIRS), ellipsometry, surface plasmon resonance (SPR), and matrix assisted laser desorption ionization (MALDI)) to establish their structure and function. The protein resistance of the films, as demonstrated by their exposure to solutions of bovine serum albumin (BSA), can be modulated by the amount of MTP grafted to the polymer, which in turn, affects their mass coverage. We show that it is possible to specifically capture hexahistidine tagged proteins with low incidences of nonspecific adsorption using these materials, a discrimination quantified using surface plasmon resonance (SPR) at concentrations down to ~20 nM. Furthermore, these polymersmore » also bind strongly to the surfaces of Au nanoparticles, stabilizing them against aggregation, providing them with a similar capacity to selectively bind 6His tagged proteins that can then be speciated using MALDI.« less

Authors:
 [1];  [1];  [1]
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  1. Univ. of Illinois at Urbana-Champaign, IL (United States)
Publication Date:
Research Org.:
Univ. of Illinois at Urbana-Champaign, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES). Materials Sciences & Engineering Division; National Science Foundation (NSF)
OSTI Identifier:
1875079
Grant/Contract Number:  
FG02-07ER46471; CHE0704153
Resource Type:
Accepted Manuscript
Journal Name:
Physical Chemistry Chemical Physics. PCCP
Additional Journal Information:
Journal Volume: 12; Journal Issue: 17; Journal ID: ISSN 1463-9076
Publisher:
Royal Society of Chemistry
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Thompson, Lucas B., Mack, Nathan H., and Nuzzo, Ralph G. Bifunctional polyacrylamide based polymers for the specific binding of hexahistidine tagged proteins on gold surfaces. United States: N. p., 2009. Web. doi:10.1039/b920713a.
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Thompson, Lucas B., Mack, Nathan H., & Nuzzo, Ralph G. Bifunctional polyacrylamide based polymers for the specific binding of hexahistidine tagged proteins on gold surfaces. United States. https://doi.org/10.1039/b920713a
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Thompson, Lucas B., Mack, Nathan H., and Nuzzo, Ralph G. Fri . "Bifunctional polyacrylamide based polymers for the specific binding of hexahistidine tagged proteins on gold surfaces". United States. https://doi.org/10.1039/b920713a. https://www.osti.gov/servlets/purl/1875079.
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@article{osti_1875079,
title = {Bifunctional polyacrylamide based polymers for the specific binding of hexahistidine tagged proteins on gold surfaces},
author = {Thompson, Lucas B. and Mack, Nathan H. and Nuzzo, Ralph G.},
abstractNote = {We describe a modified bifunctional analogue of polyacrylamide that spontaneously forms self-assembled polymeric thin films on Au surfaces. The film is engineered to specifically bind histidine tagged proteins (6His), while simultaneously remaining inherently resistant to the non-specific adsorption of proteins in solution. The backbone of a polyacrylamide-co-n-acryloxysuccinimide copolymer is functionalized via tandem active ester (NHS) couplings with 3-(methylthio)propylamine (MTP) and nitrilotriacetic acid (NTA). The resulting functionalized polymers form stable and exceptionally hydrophilic thin films that are ~2–5 nm thick, a mass coverage that varies with the MTP graft density. These films are characterized using a variety of techniques (X-ray photoelectron spectroscopy (XPS), reflection absorption infrared spectroscopy (RAIRS), ellipsometry, surface plasmon resonance (SPR), and matrix assisted laser desorption ionization (MALDI)) to establish their structure and function. The protein resistance of the films, as demonstrated by their exposure to solutions of bovine serum albumin (BSA), can be modulated by the amount of MTP grafted to the polymer, which in turn, affects their mass coverage. We show that it is possible to specifically capture hexahistidine tagged proteins with low incidences of nonspecific adsorption using these materials, a discrimination quantified using surface plasmon resonance (SPR) at concentrations down to ~20 nM. Furthermore, these polymers also bind strongly to the surfaces of Au nanoparticles, stabilizing them against aggregation, providing them with a similar capacity to selectively bind 6His tagged proteins that can then be speciated using MALDI.},
doi = {10.1039/b920713a},
journal = {Physical Chemistry Chemical Physics. PCCP},
number = 17,
volume = 12,
place = {United States},
year = {Fri Dec 04 00:00:00 EST 2009},
month = {Fri Dec 04 00:00:00 EST 2009}
}
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