Controlling Protein Surface Orientation by Strategic Placement of Oligo-Histidine Tags
We report oriented immobilization of proteins using the standard hexahistidine (His6)-Ni2+:NTA (nitrilotriacetic acid) methodology, which we systematically tuned to give control of surface coverage. Fluorescence microscopy and surface plasmon resonance measurements of self-assembled monolayers (SAMs...
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Published in | ACS nano Vol. 11; no. 9; pp. 9068 - 9083 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
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American Chemical Society
26.09.2017
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Abstract | We report oriented immobilization of proteins using the standard hexahistidine (His6)-Ni2+:NTA (nitrilotriacetic acid) methodology, which we systematically tuned to give control of surface coverage. Fluorescence microscopy and surface plasmon resonance measurements of self-assembled monolayers (SAMs) of red fluorescent proteins (TagRFP) showed that binding strength increased by 1 order of magnitude for each additional His6-tag on the TagRFP proteins. All TagRFP variants with His6-tags located on only one side of the barrel-shaped protein yielded a 1.5 times higher surface coverage compared to variants with His6-tags on opposite sides of the so-called β-barrel. Time-resolved fluorescence anisotropy measurements supported by polarized infrared spectroscopy verified that the orientation (and thus coverage and functionality) of proteins on surfaces can be controlled by strategic placement of a His6-tag on the protein. Molecular dynamics simulations show how the differently tagged proteins reside at the surface in “end-on” and “side-on” orientations with each His6-tag contributing to binding. Also, not every dihistidine subunit in a given His6-tag forms a full coordination bond with the Ni2+:NTA SAMs, which varied with the position of the His6-tag on the protein. At equal valency but different tag positions on the protein, differences in binding were caused by probing for Ni2+:NTA moieties and by additional electrostatic interactions between different fractions of the β-barrel structure and charged NTA moieties. Potential of mean force calculations indicate there is no specific single-protein interaction mode that provides a clear preferential surface orientation, suggesting that the experimentally measured preference for the end-on orientation is a supra-protein, not a single-protein, effect. |
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AbstractList | We report oriented immobilization of proteins using the standard hexahistidine (His
)-Ni
:NTA (nitrilotriacetic acid) methodology, which we systematically tuned to give control of surface coverage. Fluorescence microscopy and surface plasmon resonance measurements of self-assembled monolayers (SAMs) of red fluorescent proteins (TagRFP) showed that binding strength increased by 1 order of magnitude for each additional His
-tag on the TagRFP proteins. All TagRFP variants with His
-tags located on only one side of the barrel-shaped protein yielded a 1.5 times higher surface coverage compared to variants with His
-tags on opposite sides of the so-called β-barrel. Time-resolved fluorescence anisotropy measurements supported by polarized infrared spectroscopy verified that the orientation (and thus coverage and functionality) of proteins on surfaces can be controlled by strategic placement of a His
-tag on the protein. Molecular dynamics simulations show how the differently tagged proteins reside at the surface in "end-on" and "side-on" orientations with each His
-tag contributing to binding. Also, not every dihistidine subunit in a given His
-tag forms a full coordination bond with the Ni
:NTA SAMs, which varied with the position of the His
-tag on the protein. At equal valency but different tag positions on the protein, differences in binding were caused by probing for Ni
:NTA moieties and by additional electrostatic interactions between different fractions of the β-barrel structure and charged NTA moieties. Potential of mean force calculations indicate there is no specific single-protein interaction mode that provides a clear preferential surface orientation, suggesting that the experimentally measured preference for the end-on orientation is a supra-protein, not a single-protein, effect. We report oriented immobilization of proteins using the standard hexahistidine (His6)-Ni2+:NTA (nitrilotriacetic acid) methodology, which we systematically tuned to give control of surface coverage. Fluorescence microscopy and surface plasmon resonance measurements of self-assembled monolayers (SAMs) of red fluorescent proteins (TagRFP) showed that binding strength increased by 1 order of magnitude for each additional His6-tag on the TagRFP proteins. All TagRFP variants with His6-tags located on only one side of the barrel-shaped protein yielded a 1.5 times higher surface coverage compared to variants with His6-tags on opposite sides of the so-called β-barrel. Time-resolved fluorescence anisotropy measurements supported by polarized infrared spectroscopy verified that the orientation (and thus coverage and functionality) of proteins on surfaces can be controlled by strategic placement of a His6-tag on the protein. Molecular dynamics simulations show how the differently tagged proteins reside at the surface in “end-on” and “side-on” orientations with each His6-tag contributing to binding. Also, not every dihistidine subunit in a given His6-tag forms a full coordination bond with the Ni2+:NTA SAMs, which varied with the position of the His6-tag on the protein. At equal valency but different tag positions on the protein, differences in binding were caused by probing for Ni2+:NTA moieties and by additional electrostatic interactions between different fractions of the β-barrel structure and charged NTA moieties. Potential of mean force calculations indicate there is no specific single-protein interaction mode that provides a clear preferential surface orientation, suggesting that the experimentally measured preference for the end-on orientation is a supra-protein, not a single-protein, effect. We report oriented immobilization of proteins using the standard hexahistidine (His 6 )-Ni 2+ :NTA (nitrilotriacetic acid) methodology, which we systematically tuned to give control of surface coverage. Fluorescence microscopy and surface plasmon resonance measurements of self-assembled monolayers (SAMs) of red fluorescent proteins (TagRFP) showed that binding strength increased by 1 order of magnitude for each additional His 6 -tag on the TagRFP proteins. All TagRFP variants with His 6 -tags located on only one side of the barrel-shaped protein yielded a 1.5 times higher surface coverage compared to variants with His 6 -tags on opposite sides of the so-called β-barrel. Time-resolved fluorescence anisotropy measurements supported by polarized infrared spectroscopy verified that the orientation (and thus coverage and functionality) of proteins on surfaces can be controlled by strategic placement of a His 6 -tag on the protein. Molecular dynamics simulations show how the differently tagged proteins reside at the surface in “end-on” and “side-on” orientations with each His 6 -tag contributing to binding. Also, not every dihistidine subunit in a given His 6 -tag forms a full coordination bond with the Ni 2+ :NTA SAMs, which varied with the position of the His 6 -tag on the protein. At equal valency but different tag positions on the protein, differences in binding were caused by probing for Ni 2+ :NTA moieties and by additional electrostatic interactions between different fractions of the β-barrel structure and charged NTA moieties. Potential of mean force calculations indicate there is no specific single-protein interaction mode that provides a clear preferential surface orientation, suggesting that the experimentally measured preference for the end-on orientation is a supra -protein, not a single-protein, effect. |
Author | Wasserberg, Dorothee Prangsma, Jord Blum, Christian Jonkheijm, Pascal Subramaniam, Vinod Cazade, Pierre-Andre Cabanas-Danés, Jordi Huskens, Jurriaan Thompson, Damien O’Mahony, Shane Tromp, Eldrich |
AuthorAffiliation | University of Limerick Molecular nanoFabrication Group, MESA+ Institute for Nanotechnology Department of Physics, Bernal Institute Free University of Amsterdam Bioinspired Molecular Engineering Laboratory, MIRA Biomedical Technology and Technical Medicine Institute Nanobiophysics Group, MESA+ Institute for Nanotechnology, and MIRA Biomedical Technology and Technical Medicine Institute |
AuthorAffiliation_xml | – name: Nanobiophysics Group, MESA+ Institute for Nanotechnology, and MIRA Biomedical Technology and Technical Medicine Institute – name: – name: Molecular nanoFabrication Group, MESA+ Institute for Nanotechnology – name: Bioinspired Molecular Engineering Laboratory, MIRA Biomedical Technology and Technical Medicine Institute – name: Free University of Amsterdam – name: Department of Physics, Bernal Institute – name: University of Limerick |
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Keywords | molecular dynamics simulations self-assembly protein immobilization monolayers multivalency |
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Snippet | We report oriented immobilization of proteins using the standard hexahistidine (His6)-Ni2+:NTA (nitrilotriacetic acid) methodology, which we systematically... We report oriented immobilization of proteins using the standard hexahistidine (His )-Ni :NTA (nitrilotriacetic acid) methodology, which we systematically... We report oriented immobilization of proteins using the standard hexahistidine (His 6 )-Ni 2+ :NTA (nitrilotriacetic acid) methodology, which we systematically... |
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StartPage | 9068 |
SubjectTerms | Animals Histidine - chemistry Immobilized Proteins - chemistry Luminescent Proteins - chemistry Molecular Dynamics Simulation Nickel - chemistry Nitrilotriacetic Acid - chemistry Oligopeptides - chemistry Red Fluorescent Protein Sea Anemones - chemistry Surface Properties |
Title | Controlling Protein Surface Orientation by Strategic Placement of Oligo-Histidine Tags |
URI | http://dx.doi.org/10.1021/acsnano.7b03717 https://www.ncbi.nlm.nih.gov/pubmed/28850777 https://search.proquest.com/docview/1933941754 https://pubmed.ncbi.nlm.nih.gov/PMC5618149 |
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