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Interaction of Globular Plasma Proteins with Water-Soluble CdSe Quantum Dots
The interactions between water‐soluble semiconductor quantum dots [hydrophilic 3‐mercaptopropionic acid (MPA)‐coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β‐lactoglobulin (β‐Lg) and human serum albumin (HSA), are investigated. Acidic residues of protein molecu...
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| Published in: | Chemphyschem 2015-06, Vol.16 (8), p.1777-1786 |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c5589-37bb8fbcda265100295c5ccf57de7a0316b1b5dacb41823ef9ec04d331129f43 |
| container_end_page | 1786 |
| container_issue | 8 |
| container_start_page | 1777 |
| container_title | Chemphyschem |
| container_volume | 16 |
| creator | Pathak, Jyotsana Rawat, Kamla Sanwlani, Shilpa Bohidar, H. B. |
| description | The interactions between water‐soluble semiconductor quantum dots [hydrophilic 3‐mercaptopropionic acid (MPA)‐coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β‐lactoglobulin (β‐Lg) and human serum albumin (HSA), are investigated. Acidic residues of protein molecules form electrostatic interactions with these quantum dots (QDs). To determine the stoichiometry of proteins bound to QDs, we used dynamic light scattering (DLS) and zeta potential techniques. Fluorescence resonance energy transfer (FRET) experiments revealed energy transfer from tryptophan residues in the proteins to the QD particles. Quenching of the intrinsic fluorescence of protein molecules was noticed during this binding process (hierarchy HSA |
| doi_str_mv | 10.1002/cphc.201402629 |
| format | article |
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A complex situation: The interactions between water‐soluble semiconductor quantum dots [hydrophilic 3‐mercaptopropionic acid (MPA)‐coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β‐lactoglobulin (β‐Lg) and human serum albumin (HSA), are investigated.</description><identifier>ISSN: 1439-4235</identifier><identifier>EISSN: 1439-7641</identifier><identifier>DOI: 10.1002/cphc.201402629</identifier><identifier>PMID: 25767054</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Binding Sites ; Cadmium Compounds - chemistry ; conformation analysis ; Fluorescence ; Humans ; hydration ; Microscopy, Electron, Transmission ; Proteins ; Quantum dots ; Quantum Dots - chemistry ; Quantum Dots - metabolism ; secondary structure ; Selenium Compounds - chemistry ; Serum Albumin - chemistry ; Serum Albumin - metabolism ; Solubility ; Water - chemistry</subject><ispartof>Chemphyschem, 2015-06, Vol.16 (8), p.1777-1786</ispartof><rights>2015 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5589-37bb8fbcda265100295c5ccf57de7a0316b1b5dacb41823ef9ec04d331129f43</citedby><cites>FETCH-LOGICAL-c5589-37bb8fbcda265100295c5ccf57de7a0316b1b5dacb41823ef9ec04d331129f43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25767054$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pathak, Jyotsana</creatorcontrib><creatorcontrib>Rawat, Kamla</creatorcontrib><creatorcontrib>Sanwlani, Shilpa</creatorcontrib><creatorcontrib>Bohidar, H. B.</creatorcontrib><title>Interaction of Globular Plasma Proteins with Water-Soluble CdSe Quantum Dots</title><title>Chemphyschem</title><addtitle>ChemPhysChem</addtitle><description>The interactions between water‐soluble semiconductor quantum dots [hydrophilic 3‐mercaptopropionic acid (MPA)‐coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β‐lactoglobulin (β‐Lg) and human serum albumin (HSA), are investigated. Acidic residues of protein molecules form electrostatic interactions with these quantum dots (QDs). To determine the stoichiometry of proteins bound to QDs, we used dynamic light scattering (DLS) and zeta potential techniques. Fluorescence resonance energy transfer (FRET) experiments revealed energy transfer from tryptophan residues in the proteins to the QD particles. Quenching of the intrinsic fluorescence of protein molecules was noticed during this binding process (hierarchy HSA<β‐Lg <BSA, lower binding affinity for hydrophobic protein molecules). Upon binding with QD particles, the protein molecules underwent substantial conformational changes at the secondary‐structure level (50 % helicity lost), due to loss in hydration.
A complex situation: The interactions between water‐soluble semiconductor quantum dots [hydrophilic 3‐mercaptopropionic acid (MPA)‐coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β‐lactoglobulin (β‐Lg) and human serum albumin (HSA), are investigated.</description><subject>Binding Sites</subject><subject>Cadmium Compounds - chemistry</subject><subject>conformation analysis</subject><subject>Fluorescence</subject><subject>Humans</subject><subject>hydration</subject><subject>Microscopy, Electron, Transmission</subject><subject>Proteins</subject><subject>Quantum dots</subject><subject>Quantum Dots - chemistry</subject><subject>Quantum Dots - metabolism</subject><subject>secondary structure</subject><subject>Selenium Compounds - chemistry</subject><subject>Serum Albumin - chemistry</subject><subject>Serum Albumin - metabolism</subject><subject>Solubility</subject><subject>Water - chemistry</subject><issn>1439-4235</issn><issn>1439-7641</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><recordid>eNqFkD1PwzAYhC0E4ntlRJZYWFL8GScjBChIFRSB1NGyHUcEnLjYiYB_T0pLhViY3nd47nR3ABxhNMIIkTMzfzYjgjBDJCX5BtjFjOaJSBneXP2MUL4D9mJ8QQhlSOBtsEO4SAXibBdMbtvOBmW62rfQV3DsvO6dCnDqVGwUnAbf2bqN8L3unuFMDXDy6F2vnYVF-WjhQ6_arm_gpe_iAdiqlIv2cHX3wdP11VNxk0zux7fF-SQxnGd5QoXWWaVNqUjKFy1ybrgxFRelFQpRnGqseamMZjgj1Fa5NYiVlGJM8orRfXC6tJ0H_9bb2MmmjsY6p1rr-yhxmlExNMQL9OQP-uL70A7hvilKEKV8oEZLygQfY7CVnIe6UeFTYiQXAeViZrmeeRAcr2x73dhyjf_sOgD5Enivnf38x04W05vit3my1Naxsx9rrQqvMhVDMTm7G8vLi-lszK4LmdEvONGXSA</recordid><startdate>20150608</startdate><enddate>20150608</enddate><creator>Pathak, Jyotsana</creator><creator>Rawat, Kamla</creator><creator>Sanwlani, Shilpa</creator><creator>Bohidar, H. 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B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5589-37bb8fbcda265100295c5ccf57de7a0316b1b5dacb41823ef9ec04d331129f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Binding Sites</topic><topic>Cadmium Compounds - chemistry</topic><topic>conformation analysis</topic><topic>Fluorescence</topic><topic>Humans</topic><topic>hydration</topic><topic>Microscopy, Electron, Transmission</topic><topic>Proteins</topic><topic>Quantum dots</topic><topic>Quantum Dots - chemistry</topic><topic>Quantum Dots - metabolism</topic><topic>secondary structure</topic><topic>Selenium Compounds - chemistry</topic><topic>Serum Albumin - chemistry</topic><topic>Serum Albumin - metabolism</topic><topic>Solubility</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pathak, Jyotsana</creatorcontrib><creatorcontrib>Rawat, Kamla</creatorcontrib><creatorcontrib>Sanwlani, Shilpa</creatorcontrib><creatorcontrib>Bohidar, H. 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B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of Globular Plasma Proteins with Water-Soluble CdSe Quantum Dots</atitle><jtitle>Chemphyschem</jtitle><addtitle>ChemPhysChem</addtitle><date>2015-06-08</date><risdate>2015</risdate><volume>16</volume><issue>8</issue><spage>1777</spage><epage>1786</epage><pages>1777-1786</pages><issn>1439-4235</issn><eissn>1439-7641</eissn><abstract>The interactions between water‐soluble semiconductor quantum dots [hydrophilic 3‐mercaptopropionic acid (MPA)‐coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β‐lactoglobulin (β‐Lg) and human serum albumin (HSA), are investigated. Acidic residues of protein molecules form electrostatic interactions with these quantum dots (QDs). To determine the stoichiometry of proteins bound to QDs, we used dynamic light scattering (DLS) and zeta potential techniques. Fluorescence resonance energy transfer (FRET) experiments revealed energy transfer from tryptophan residues in the proteins to the QD particles. Quenching of the intrinsic fluorescence of protein molecules was noticed during this binding process (hierarchy HSA<β‐Lg <BSA, lower binding affinity for hydrophobic protein molecules). Upon binding with QD particles, the protein molecules underwent substantial conformational changes at the secondary‐structure level (50 % helicity lost), due to loss in hydration.
A complex situation: The interactions between water‐soluble semiconductor quantum dots [hydrophilic 3‐mercaptopropionic acid (MPA)‐coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β‐lactoglobulin (β‐Lg) and human serum albumin (HSA), are investigated.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>25767054</pmid><doi>10.1002/cphc.201402629</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Chemphyschem, 2015-06, Vol.16 (8), p.1777-1786 |
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| subjects | Binding Sites Cadmium Compounds - chemistry conformation analysis Fluorescence Humans hydration Microscopy, Electron, Transmission Proteins Quantum dots Quantum Dots - chemistry Quantum Dots - metabolism secondary structure Selenium Compounds - chemistry Serum Albumin - chemistry Serum Albumin - metabolism Solubility Water - chemistry |
| title | Interaction of Globular Plasma Proteins with Water-Soluble CdSe Quantum Dots |
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