Near-Field Scanning Optical Microscopy Measurements of Fluorescent Molecular Probes Binding to Insulin Amyloid Fibrils
The binding of two amyloid fibril stain dyes, thioflavin T (ThT) and its neutral analog 2-[4′-(dimethylamino)phenyl]-benzothiazole (BTA-2), are measured using near-field scanning optical microscopy (NSOM), which is able to image individual amyloid fibrils. Polarized NSOM images reveal that both dyes...
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| Veröffentlicht in: | The journal of physical chemistry. B 2009-09, Vol.113 (35), p.12090-12095 |
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| container_title | The journal of physical chemistry. B |
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| creator | Kitts, Catherine C Bout, David A. Vanden |
| description | The binding of two amyloid fibril stain dyes, thioflavin T (ThT) and its neutral analog 2-[4′-(dimethylamino)phenyl]-benzothiazole (BTA-2), are measured using near-field scanning optical microscopy (NSOM), which is able to image individual amyloid fibrils. Polarized NSOM images reveal that both dyes bind to the fibrils with the long axis of the molecule aligned parallel to the long axis of the fibrils. This indicates that the dyes bind along the surface of the β-sheet within the grooves of the fibril that run parallel to the fibril axis. The similarity in the binding motifs of the two dyes shows that electrostatic interaction of the charged amine group on the ThT dye plays a minimal role in the affinity of the dyes for the amyloids. The polarized NSOM images confirm that the enhanced fluorescence of the ThT and BTA-2 result from binding of the monomeric dye rather than micelles or excimer species. |
| doi_str_mv | 10.1021/jp903509u |
| format | Article |
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Vanden</creatorcontrib><title>Near-Field Scanning Optical Microscopy Measurements of Fluorescent Molecular Probes Binding to Insulin Amyloid Fibrils</title><title>The journal of physical chemistry. B</title><addtitle>J. Phys. Chem. B</addtitle><description>The binding of two amyloid fibril stain dyes, thioflavin T (ThT) and its neutral analog 2-[4′-(dimethylamino)phenyl]-benzothiazole (BTA-2), are measured using near-field scanning optical microscopy (NSOM), which is able to image individual amyloid fibrils. Polarized NSOM images reveal that both dyes bind to the fibrils with the long axis of the molecule aligned parallel to the long axis of the fibrils. This indicates that the dyes bind along the surface of the β-sheet within the grooves of the fibril that run parallel to the fibril axis. The similarity in the binding motifs of the two dyes shows that electrostatic interaction of the charged amine group on the ThT dye plays a minimal role in the affinity of the dyes for the amyloids. The polarized NSOM images confirm that the enhanced fluorescence of the ThT and BTA-2 result from binding of the monomeric dye rather than micelles or excimer species.</description><subject>Amyloid - chemistry</subject><subject>Aniline Compounds - chemistry</subject><subject>Animals</subject><subject>B: Biophysical Chemistry</subject><subject>Benzothiazoles - chemistry</subject><subject>Biophysics - methods</subject><subject>Cattle</subject><subject>Fluorescent Dyes - chemistry</subject><subject>Fluorescent Dyes - pharmacology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Insulin - chemistry</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Micelles</subject><subject>Microscopy, Atomic Force - methods</subject><subject>Microscopy, Fluorescence - instrumentation</subject><subject>Microscopy, Fluorescence - methods</subject><subject>Protein Binding</subject><subject>Thiazoles - chemistry</subject><issn>1520-6106</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE9LxDAQxYMo_j_4BSQXBQ_VpN1km6OKq4KrgnouaTKVLGlSk0bYb2-WXfQiwzBv4Mdj5iF0QsklJSW9WgyCVIyItIX2KStJkXu6vdGcEr6HDmJcEFKysua7aI8KzqsJKffR9zPIUMwMWI3flHTOuE_8MoxGSYvnRgUflR-WeA4ypgA9uDFi3-GZTT5AVHnHc29BJSsDfg2-hYhvjNMrn9HjRxeTNQ5f90vrjcYz0wZj4xHa6aSNcLyZh-hjdvd--1A8vdw_3l4_FbKairGoqBAtUGAtrVuoWs6zFKoELnLVQmlJdSfKalLLeiLLrtMMlNZT1klGSVsdovO17xD8V4I4Nr3JR1srHfgUGz7llFWMZvBiDa4-jgG6Zgiml2HZUNKsQm5-Q87s6cY0tT3oP3KTagbO1oBUsVn4FFz-8R-jH0rYhZg</recordid><startdate>20090903</startdate><enddate>20090903</enddate><creator>Kitts, Catherine C</creator><creator>Bout, David A. 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Vanden</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The journal of physical chemistry. B</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kitts, Catherine C</au><au>Bout, David A. Vanden</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Near-Field Scanning Optical Microscopy Measurements of Fluorescent Molecular Probes Binding to Insulin Amyloid Fibrils</atitle><jtitle>The journal of physical chemistry. B</jtitle><addtitle>J. Phys. Chem. B</addtitle><date>2009-09-03</date><risdate>2009</risdate><volume>113</volume><issue>35</issue><spage>12090</spage><epage>12095</epage><pages>12090-12095</pages><issn>1520-6106</issn><eissn>1520-5207</eissn><abstract>The binding of two amyloid fibril stain dyes, thioflavin T (ThT) and its neutral analog 2-[4′-(dimethylamino)phenyl]-benzothiazole (BTA-2), are measured using near-field scanning optical microscopy (NSOM), which is able to image individual amyloid fibrils. Polarized NSOM images reveal that both dyes bind to the fibrils with the long axis of the molecule aligned parallel to the long axis of the fibrils. This indicates that the dyes bind along the surface of the β-sheet within the grooves of the fibril that run parallel to the fibril axis. The similarity in the binding motifs of the two dyes shows that electrostatic interaction of the charged amine group on the ThT dye plays a minimal role in the affinity of the dyes for the amyloids. The polarized NSOM images confirm that the enhanced fluorescence of the ThT and BTA-2 result from binding of the monomeric dye rather than micelles or excimer species.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>19663402</pmid><doi>10.1021/jp903509u</doi><tpages>6</tpages></addata></record> |
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| subjects | Amyloid - chemistry Aniline Compounds - chemistry Animals B: Biophysical Chemistry Benzothiazoles - chemistry Biophysics - methods Cattle Fluorescent Dyes - chemistry Fluorescent Dyes - pharmacology Hydrogen-Ion Concentration Insulin - chemistry Magnetic Resonance Spectroscopy Micelles Microscopy, Atomic Force - methods Microscopy, Fluorescence - instrumentation Microscopy, Fluorescence - methods Protein Binding Thiazoles - chemistry |
| title | Near-Field Scanning Optical Microscopy Measurements of Fluorescent Molecular Probes Binding to Insulin Amyloid Fibrils |
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