Protein Adsorption Orientation in the Light of Fluorescent Probes: Mapping of the Interaction between Site-Directly Labeled Human Carbonic Anhydrase II and Silica Nanoparticles

Little is known about the direction and specificity of protein adsorption to solid surfaces, a knowledge that is of great importance in many biotechnological applications. To resolve the direction in which a protein with known structure and surface potentials binds to negatively charged silica nanop...

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Published in:Biophysical journal 2005-05, Vol.88 (5), p.3536-3544
Main Authors: Karlsson, Martin, Carlsson, Uno
Format: Article
Language:English
Subjects:
Acrylamide - pharmacology
Adsorption
Anisotropy
Arginine - chemistry
Biotechnology
Carbonic Anhydrase II - chemistry
Chromatography, Gel
Circular Dichroism
Escherichia coli - metabolism
Fluorescence
Fluorescent Dyes - pharmacology
Histidine - chemistry
Humans
Hydrogen-Ion Concentration
Lysine - chemistry
Mapping
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Nanoparticles
Naphthalenesulfonates - pharmacology
NATURAL SCIENCES
NATURVETENSKAP
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Proteins
Proteins - chemistry
Silica
Silicon - chemistry
Software
Spectrometry, Fluorescence
Spectrophotometry
Sulfhydryl Compounds - chemistry
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cited_by cdi_FETCH-LOGICAL-c587t-31d3dc98dd2d52e7cdab766cbda6e2be59b9bf07b0c092f6b603e21e0f35c8f63
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description Little is known about the direction and specificity of protein adsorption to solid surfaces, a knowledge that is of great importance in many biotechnological applications. To resolve the direction in which a protein with known structure and surface potentials binds to negatively charged silica nanoparticles, fluorescent probes were attached to different areas on the surface of the protein human carbonic anhydrase II. By this approach it was clearly demonstrated that the adsorption of the native protein is specific to limited regions at the surface of the N-terminal domain of the protein. Furthermore, the adsorption direction is strongly pH-dependent. At pH 6.3, a histidine-rich area around position 10 is the dominating adsorption region. At higher pH values, when the histidines in this area are deprotonated, the protein is also adsorbed by a region close to position 37, which contains several lysines and arginines. Clearly the adsorption is directed by positively charged areas on the protein surface toward the negatively charged silica surface at conditions when specific binding occurs.
doi_str_mv 10.1529/biophysj.104.054809
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subjects Acrylamide - pharmacology
Adsorption
Anisotropy
Arginine - chemistry
Biotechnology
Carbonic Anhydrase II - chemistry
Chromatography, Gel
Circular Dichroism
Escherichia coli - metabolism
Fluorescence
Fluorescent Dyes - pharmacology
Histidine - chemistry
Humans
Hydrogen-Ion Concentration
Lysine - chemistry
Mapping
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Nanoparticles
Naphthalenesulfonates - pharmacology
NATURAL SCIENCES
NATURVETENSKAP
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Proteins
Proteins - chemistry
Silica
Silicon - chemistry
Software
Spectrometry, Fluorescence
Spectrophotometry
Sulfhydryl Compounds - chemistry
title Protein Adsorption Orientation in the Light of Fluorescent Probes: Mapping of the Interaction between Site-Directly Labeled Human Carbonic Anhydrase II and Silica Nanoparticles
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