Gold nanoparticle-based tool to study protein conformational variants: implications in hemoglobinopathy
Abstract The size of gold nanoparticles is shown here to gradually decrease if it is allowed to grow on a protein template, and the protein is subjected to unfolding by a nonionic denaturant. The correlation between size of the gold nanoparticle formed and the plasmon frequency observed remains line...
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| Veröffentlicht in: | Nanomedicine 2007-03, Vol.3 (1), p.14-19 |
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| creator | Bhattacharya, Jaydeep, MTech Jasrapuria, Sinu, MSc Sarkar, Tapan, MSc GhoshMoulick, Ranjita, MSc Dasgupta, Anjan Kr., PhD |
| description | Abstract The size of gold nanoparticles is shown here to gradually decrease if it is allowed to grow on a protein template, and the protein is subjected to unfolding by a nonionic denaturant. The correlation between size of the gold nanoparticle formed and the plasmon frequency observed remains linear, except at stages where protein folding intermediates are formed. Higher population of exposed tyrosine residues, number of sulfhydryl groups of the protein, and the overall exposition of the inner hydrophobic core may lead to the generation of smaller particles. The method provides a simple colorimetric sensing of protein conformation and has been tested for both nonheme and heme proteins (hemoglobin and bovine serum albumin). Similarly, protein variants with defects in folding (caused by subunit misassembly or mutation) can also be classified. Possible application of this approach in hemoglobinopathy (e.g., thalassemia carrier detection) is discussed in the text. |
| doi_str_mv | 10.1016/j.nano.2006.10.159 |
| format | Article |
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The correlation between size of the gold nanoparticle formed and the plasmon frequency observed remains linear, except at stages where protein folding intermediates are formed. Higher population of exposed tyrosine residues, number of sulfhydryl groups of the protein, and the overall exposition of the inner hydrophobic core may lead to the generation of smaller particles. The method provides a simple colorimetric sensing of protein conformation and has been tested for both nonheme and heme proteins (hemoglobin and bovine serum albumin). Similarly, protein variants with defects in folding (caused by subunit misassembly or mutation) can also be classified. Possible application of this approach in hemoglobinopathy (e.g., thalassemia carrier detection) is discussed in the text.</description><identifier>ISSN: 1549-9634</identifier><identifier>EISSN: 1549-9642</identifier><identifier>DOI: 10.1016/j.nano.2006.10.159</identifier><identifier>PMID: 17379165</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cattle ; Fluorescence ; Folding ; Gold ; Gold nanoparticle ; Hemoglobin ; Hemoglobinopathies - pathology ; Hemoglobinopathy ; Hemoglobins - chemistry ; Hemoglobins - metabolism ; Humans ; Internal Medicine ; Nanoparticles ; Particle Size ; Plasmon resonance ; Protein Conformation ; Protein Folding ; Serum albumin ; Serum Albumin, Bovine - chemistry ; Serum Albumin, Bovine - metabolism ; Surface Plasmon Resonance ; Tryptophan ; Tyrosine ; Urea</subject><ispartof>Nanomedicine, 2007-03, Vol.3 (1), p.14-19</ispartof><rights>2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-d8a78220dd541c56426cfc40b80339509052eb0141aa6e4788a9882a24565d883</citedby><cites>FETCH-LOGICAL-c440t-d8a78220dd541c56426cfc40b80339509052eb0141aa6e4788a9882a24565d883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.nano.2006.10.159$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17379165$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bhattacharya, Jaydeep, MTech</creatorcontrib><creatorcontrib>Jasrapuria, Sinu, MSc</creatorcontrib><creatorcontrib>Sarkar, Tapan, MSc</creatorcontrib><creatorcontrib>GhoshMoulick, Ranjita, MSc</creatorcontrib><creatorcontrib>Dasgupta, Anjan Kr., PhD</creatorcontrib><title>Gold nanoparticle-based tool to study protein conformational variants: implications in hemoglobinopathy</title><title>Nanomedicine</title><addtitle>Nanomedicine</addtitle><description>Abstract The size of gold nanoparticles is shown here to gradually decrease if it is allowed to grow on a protein template, and the protein is subjected to unfolding by a nonionic denaturant. The correlation between size of the gold nanoparticle formed and the plasmon frequency observed remains linear, except at stages where protein folding intermediates are formed. Higher population of exposed tyrosine residues, number of sulfhydryl groups of the protein, and the overall exposition of the inner hydrophobic core may lead to the generation of smaller particles. The method provides a simple colorimetric sensing of protein conformation and has been tested for both nonheme and heme proteins (hemoglobin and bovine serum albumin). Similarly, protein variants with defects in folding (caused by subunit misassembly or mutation) can also be classified. Possible application of this approach in hemoglobinopathy (e.g., thalassemia carrier detection) is discussed in the text.</description><subject>Animals</subject><subject>Cattle</subject><subject>Fluorescence</subject><subject>Folding</subject><subject>Gold</subject><subject>Gold nanoparticle</subject><subject>Hemoglobin</subject><subject>Hemoglobinopathies - pathology</subject><subject>Hemoglobinopathy</subject><subject>Hemoglobins - chemistry</subject><subject>Hemoglobins - metabolism</subject><subject>Humans</subject><subject>Internal Medicine</subject><subject>Nanoparticles</subject><subject>Particle Size</subject><subject>Plasmon resonance</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Serum albumin</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Serum Albumin, Bovine - metabolism</subject><subject>Surface Plasmon Resonance</subject><subject>Tryptophan</subject><subject>Tyrosine</subject><subject>Urea</subject><issn>1549-9634</issn><issn>1549-9642</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUsGKFDEUbERx19Uf8CB98tbjSzrpTkSEZdFVWPCgnkM6ebObMd0Zk_TC_L3JzqDgQS9JKKqKvKrXNC8JbAiQ4c1us-glbCjAsKkYl4-ac8KZ7OTA6OPf756dNc9S2gH0I4B82pyRsR8lGfh5c3sdvG2rz17H7IzHbtIJbZtD8OVoU17tod3HkNEtrQnLNsRZZxcW7dt7HZ1ecnrbunnvnXnAU1uIdziHWx8mV43z3eF582SrfcIXp_ui-f7xw7erT93Nl-vPV5c3nWEMcmeFHgWlYC1nxPAyxmC2hsEkoO8lBwmc4gSEEa0HZKMQWgpBNWV84FaI_qJ5ffQtP_65Yspqdsmg93rBsCY1ApVyHPr_EonsBTBSHemRaGJIKeJW7aObdTwoAqr2oHaq5qdqDw8Yl0X06uS-TjPaP5JT8IXw7kjAEsa9w6iScbgYtC6iycoG92__93_JjXdLKcD_wAOmXVhj6adMoRJVoL7WTaiLAAPUAEj_C-YCrzc</recordid><startdate>20070301</startdate><enddate>20070301</enddate><creator>Bhattacharya, Jaydeep, MTech</creator><creator>Jasrapuria, Sinu, MSc</creator><creator>Sarkar, Tapan, MSc</creator><creator>GhoshMoulick, Ranjita, MSc</creator><creator>Dasgupta, Anjan Kr., PhD</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20070301</creationdate><title>Gold nanoparticle-based tool to study protein conformational variants: implications in hemoglobinopathy</title><author>Bhattacharya, Jaydeep, MTech ; Jasrapuria, Sinu, MSc ; Sarkar, Tapan, MSc ; GhoshMoulick, Ranjita, MSc ; Dasgupta, Anjan Kr., PhD</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-d8a78220dd541c56426cfc40b80339509052eb0141aa6e4788a9882a24565d883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Fluorescence</topic><topic>Folding</topic><topic>Gold</topic><topic>Gold nanoparticle</topic><topic>Hemoglobin</topic><topic>Hemoglobinopathies - pathology</topic><topic>Hemoglobinopathy</topic><topic>Hemoglobins - chemistry</topic><topic>Hemoglobins - metabolism</topic><topic>Humans</topic><topic>Internal Medicine</topic><topic>Nanoparticles</topic><topic>Particle Size</topic><topic>Plasmon resonance</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Serum albumin</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Serum Albumin, Bovine - metabolism</topic><topic>Surface Plasmon Resonance</topic><topic>Tryptophan</topic><topic>Tyrosine</topic><topic>Urea</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bhattacharya, Jaydeep, MTech</creatorcontrib><creatorcontrib>Jasrapuria, Sinu, MSc</creatorcontrib><creatorcontrib>Sarkar, Tapan, MSc</creatorcontrib><creatorcontrib>GhoshMoulick, Ranjita, MSc</creatorcontrib><creatorcontrib>Dasgupta, Anjan Kr., PhD</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nanomedicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bhattacharya, Jaydeep, MTech</au><au>Jasrapuria, Sinu, MSc</au><au>Sarkar, Tapan, MSc</au><au>GhoshMoulick, Ranjita, MSc</au><au>Dasgupta, Anjan Kr., PhD</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gold nanoparticle-based tool to study protein conformational variants: implications in hemoglobinopathy</atitle><jtitle>Nanomedicine</jtitle><addtitle>Nanomedicine</addtitle><date>2007-03-01</date><risdate>2007</risdate><volume>3</volume><issue>1</issue><spage>14</spage><epage>19</epage><pages>14-19</pages><issn>1549-9634</issn><eissn>1549-9642</eissn><abstract>Abstract The size of gold nanoparticles is shown here to gradually decrease if it is allowed to grow on a protein template, and the protein is subjected to unfolding by a nonionic denaturant. The correlation between size of the gold nanoparticle formed and the plasmon frequency observed remains linear, except at stages where protein folding intermediates are formed. Higher population of exposed tyrosine residues, number of sulfhydryl groups of the protein, and the overall exposition of the inner hydrophobic core may lead to the generation of smaller particles. The method provides a simple colorimetric sensing of protein conformation and has been tested for both nonheme and heme proteins (hemoglobin and bovine serum albumin). Similarly, protein variants with defects in folding (caused by subunit misassembly or mutation) can also be classified. Possible application of this approach in hemoglobinopathy (e.g., thalassemia carrier detection) is discussed in the text.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17379165</pmid><doi>10.1016/j.nano.2006.10.159</doi><tpages>6</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Cattle Fluorescence Folding Gold Gold nanoparticle Hemoglobin Hemoglobinopathies - pathology Hemoglobinopathy Hemoglobins - chemistry Hemoglobins - metabolism Humans Internal Medicine Nanoparticles Particle Size Plasmon resonance Protein Conformation Protein Folding Serum albumin Serum Albumin, Bovine - chemistry Serum Albumin, Bovine - metabolism Surface Plasmon Resonance Tryptophan Tyrosine Urea |
| title | Gold nanoparticle-based tool to study protein conformational variants: implications in hemoglobinopathy |
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