Dependence of phthalocyanine-based fluorescence on albumin structure: A fluorescent probe for ascorbic acid
[Display omitted] •An albumin-encapsulated fluorescence probe for ascorbic acid: the probe consists of an SiPc fluorophore and TEMPO radicals.•The fluorescence intensity reflects the structural changes of serum albumin, such as folding ↔ unfolding and α-helix ↔ β-sheet.•Usefullness for developing fl...
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| Veröffentlicht in: | Journal of photochemistry and photobiology. A, Chemistry. Chemistry., 2018-09, Vol.364, p.1-5 |
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| container_title | Journal of photochemistry and photobiology. A, Chemistry. |
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| creator | Yokoi, Takanori Ishii, Kazuyuki |
| description | [Display omitted]
•An albumin-encapsulated fluorescence probe for ascorbic acid: the probe consists of an SiPc fluorophore and TEMPO radicals.•The fluorescence intensity reflects the structural changes of serum albumin, such as folding ↔ unfolding and α-helix ↔ β-sheet.•Usefullness for developing fluorescent probes using the structural change of albumin.
In this study, we have investigated the environmental dependence of the fluorescent probe for detecting ascorbic acid. The fluorescent probe used herein, R2c, consists of silicon phthalocyanine and two 2,2,6,6-tetramethyl-1-piperidinyloxy radicals, and is encapsulated by the dimer of bovine serum albumin (BSA). Due to this encapsulation, the R2c@(BSA)2 complex was prevented from reacting with various redox species in biological systems, but reacted selectively with ascorbic acid. The fluorescence of R2c@(BSA)2 after ascorbic acid addition depended on the pH: the fluorescence intensity increased in the order pH 6 |
| doi_str_mv | 10.1016/j.jphotochem.2018.05.036 |
| format | Article |
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•An albumin-encapsulated fluorescence probe for ascorbic acid: the probe consists of an SiPc fluorophore and TEMPO radicals.•The fluorescence intensity reflects the structural changes of serum albumin, such as folding ↔ unfolding and α-helix ↔ β-sheet.•Usefullness for developing fluorescent probes using the structural change of albumin.
In this study, we have investigated the environmental dependence of the fluorescent probe for detecting ascorbic acid. The fluorescent probe used herein, R2c, consists of silicon phthalocyanine and two 2,2,6,6-tetramethyl-1-piperidinyloxy radicals, and is encapsulated by the dimer of bovine serum albumin (BSA). Due to this encapsulation, the R2c@(BSA)2 complex was prevented from reacting with various redox species in biological systems, but reacted selectively with ascorbic acid. The fluorescence of R2c@(BSA)2 after ascorbic acid addition depended on the pH: the fluorescence intensity increased in the order pH 6 < pH 5 < pH 4 < pH 3, but decreased at pH 2 compared with that at pH 3. This pH dependence was analyzed in terms of the relationship between the shielding effects of BSA and the folding ↔ unfolding structural changes. Furthermore, the fluorescence intensity of R2c@(BSA)2 decreased with increasing temperature after ascorbic acid addition, which was explained by the change in relative proportions of α-helix and β-sheet in BSA. This result will be useful for developing a fluorescent probe using the structural changes of albumin.</description><identifier>ISSN: 1010-6030</identifier><identifier>EISSN: 1873-2666</identifier><identifier>DOI: 10.1016/j.jphotochem.2018.05.036</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Ascorbic acid ; Bovine serum albumin ; Dependence ; Dimers ; Encapsulation ; Fluorescence ; Fluorescence probe ; Fluorescent indicators ; Organic chemicals ; pH effects ; Phthalocyanine ; Radical ; Serum albumin ; Shielding ; Vitamin C</subject><ispartof>Journal of photochemistry and photobiology. A, Chemistry., 2018-09, Vol.364, p.1-5</ispartof><rights>2018 Elsevier B.V.</rights><rights>Copyright Elsevier BV Sep 1, 2018</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-f3f68d28d85c53f91313f7369fd11c77876ce540b5f6ecff41d4eff13677ba4b3</citedby><cites>FETCH-LOGICAL-c412t-f3f68d28d85c53f91313f7369fd11c77876ce540b5f6ecff41d4eff13677ba4b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jphotochem.2018.05.036$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids></links><search><creatorcontrib>Yokoi, Takanori</creatorcontrib><creatorcontrib>Ishii, Kazuyuki</creatorcontrib><title>Dependence of phthalocyanine-based fluorescence on albumin structure: A fluorescent probe for ascorbic acid</title><title>Journal of photochemistry and photobiology. A, Chemistry.</title><description>[Display omitted]
•An albumin-encapsulated fluorescence probe for ascorbic acid: the probe consists of an SiPc fluorophore and TEMPO radicals.•The fluorescence intensity reflects the structural changes of serum albumin, such as folding ↔ unfolding and α-helix ↔ β-sheet.•Usefullness for developing fluorescent probes using the structural change of albumin.
In this study, we have investigated the environmental dependence of the fluorescent probe for detecting ascorbic acid. The fluorescent probe used herein, R2c, consists of silicon phthalocyanine and two 2,2,6,6-tetramethyl-1-piperidinyloxy radicals, and is encapsulated by the dimer of bovine serum albumin (BSA). Due to this encapsulation, the R2c@(BSA)2 complex was prevented from reacting with various redox species in biological systems, but reacted selectively with ascorbic acid. The fluorescence of R2c@(BSA)2 after ascorbic acid addition depended on the pH: the fluorescence intensity increased in the order pH 6 < pH 5 < pH 4 < pH 3, but decreased at pH 2 compared with that at pH 3. This pH dependence was analyzed in terms of the relationship between the shielding effects of BSA and the folding ↔ unfolding structural changes. Furthermore, the fluorescence intensity of R2c@(BSA)2 decreased with increasing temperature after ascorbic acid addition, which was explained by the change in relative proportions of α-helix and β-sheet in BSA. This result will be useful for developing a fluorescent probe using the structural changes of albumin.</description><subject>Ascorbic acid</subject><subject>Bovine serum albumin</subject><subject>Dependence</subject><subject>Dimers</subject><subject>Encapsulation</subject><subject>Fluorescence</subject><subject>Fluorescence probe</subject><subject>Fluorescent indicators</subject><subject>Organic chemicals</subject><subject>pH effects</subject><subject>Phthalocyanine</subject><subject>Radical</subject><subject>Serum albumin</subject><subject>Shielding</subject><subject>Vitamin C</subject><issn>1010-6030</issn><issn>1873-2666</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNqFkMtOwzAQRSMEEqXwD5ZYJ3hix07ZlfKUKrGBteXYY9WhjYOdIPXvSVUk2LGaWZw7j5NlBGgBFMRNW7T9JgzBbHBXlBTqglYFZeIkm0EtWV4KIU6nngLNBWX0PLtIqaWUcs5hln3cY4-dxc4gCY70m2Gjt8Hsdec7zBud0BK3HUPEZI5QR_S2GXe-I2mIoxnGiLdk-QcaSB9Dg8SFSHQyITbeEG28vczOnN4mvPqp8-z98eFt9ZyvX59eVst1bjiUQ-6YE7Uta1tXpmJuAQyYk0wsnAUwUtZSGKw4bSon0DjHwXJ0DpiQstG8YfPs-jh3uuNzxDSoNoyxm1aqEkAuSiEZn6j6SJkYUoroVB_9Tse9AqoOalWrftWqg1pFKzWpnaJ3xyhOX3x5jCoZf7BjfUQzKBv8_0O-AYtjiYE</recordid><startdate>20180901</startdate><enddate>20180901</enddate><creator>Yokoi, Takanori</creator><creator>Ishii, Kazuyuki</creator><general>Elsevier B.V</general><general>Elsevier BV</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope></search><sort><creationdate>20180901</creationdate><title>Dependence of phthalocyanine-based fluorescence on albumin structure: A fluorescent probe for ascorbic acid</title><author>Yokoi, Takanori ; Ishii, Kazuyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-f3f68d28d85c53f91313f7369fd11c77876ce540b5f6ecff41d4eff13677ba4b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Ascorbic acid</topic><topic>Bovine serum albumin</topic><topic>Dependence</topic><topic>Dimers</topic><topic>Encapsulation</topic><topic>Fluorescence</topic><topic>Fluorescence probe</topic><topic>Fluorescent indicators</topic><topic>Organic chemicals</topic><topic>pH effects</topic><topic>Phthalocyanine</topic><topic>Radical</topic><topic>Serum albumin</topic><topic>Shielding</topic><topic>Vitamin C</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yokoi, Takanori</creatorcontrib><creatorcontrib>Ishii, Kazuyuki</creatorcontrib><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of photochemistry and photobiology. A, Chemistry.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yokoi, Takanori</au><au>Ishii, Kazuyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dependence of phthalocyanine-based fluorescence on albumin structure: A fluorescent probe for ascorbic acid</atitle><jtitle>Journal of photochemistry and photobiology. A, Chemistry.</jtitle><date>2018-09-01</date><risdate>2018</risdate><volume>364</volume><spage>1</spage><epage>5</epage><pages>1-5</pages><issn>1010-6030</issn><eissn>1873-2666</eissn><abstract>[Display omitted]
•An albumin-encapsulated fluorescence probe for ascorbic acid: the probe consists of an SiPc fluorophore and TEMPO radicals.•The fluorescence intensity reflects the structural changes of serum albumin, such as folding ↔ unfolding and α-helix ↔ β-sheet.•Usefullness for developing fluorescent probes using the structural change of albumin.
In this study, we have investigated the environmental dependence of the fluorescent probe for detecting ascorbic acid. The fluorescent probe used herein, R2c, consists of silicon phthalocyanine and two 2,2,6,6-tetramethyl-1-piperidinyloxy radicals, and is encapsulated by the dimer of bovine serum albumin (BSA). Due to this encapsulation, the R2c@(BSA)2 complex was prevented from reacting with various redox species in biological systems, but reacted selectively with ascorbic acid. The fluorescence of R2c@(BSA)2 after ascorbic acid addition depended on the pH: the fluorescence intensity increased in the order pH 6 < pH 5 < pH 4 < pH 3, but decreased at pH 2 compared with that at pH 3. This pH dependence was analyzed in terms of the relationship between the shielding effects of BSA and the folding ↔ unfolding structural changes. Furthermore, the fluorescence intensity of R2c@(BSA)2 decreased with increasing temperature after ascorbic acid addition, which was explained by the change in relative proportions of α-helix and β-sheet in BSA. This result will be useful for developing a fluorescent probe using the structural changes of albumin.</abstract><cop>Lausanne</cop><pub>Elsevier B.V</pub><doi>10.1016/j.jphotochem.2018.05.036</doi><tpages>5</tpages></addata></record> |
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| subjects | Ascorbic acid Bovine serum albumin Dependence Dimers Encapsulation Fluorescence Fluorescence probe Fluorescent indicators Organic chemicals pH effects Phthalocyanine Radical Serum albumin Shielding Vitamin C |
| title | Dependence of phthalocyanine-based fluorescence on albumin structure: A fluorescent probe for ascorbic acid |
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