Fluorescence Study of the Membrane Effects of Aggregated Lysozyme
The last decade has seen unprecedented upsurge of interest in the structural and toxic properties of particular type of protein aggregates, amyloid fibrils, associated with a number of pathological states. In the present study fluorescence spectroscopy technique has been employed to gain further ins...
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| Veröffentlicht in: | Journal of fluorescence 2013-11, Vol.23 (6), p.1229-1237 |
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| creator | Kutsenko, Olga K. Trusova, Valeriya M. Gorbenko, Galyna P. Lipovaya, Anna S. Slobozhanina, Ekaterina I. Lukyanenko, Lyudmila M. Deligeorgiev, Todor Vasilev, Aleksey |
| description | The last decade has seen unprecedented upsurge of interest in the structural and toxic properties of particular type of protein aggregates, amyloid fibrils, associated with a number of pathological states. In the present study fluorescence spectroscopy technique has been employed to gain further insight into the membrane-related mechanisms of amyloid toxicity. To this end, erythrocyte model system composed of liposomes and hemoglobin was subjected to the action of oligomeric and fibrillar lysozyme. Acrylamide quenching of lysozyme fluorescence showed that solvent accessibility of Trp
62
and Trp
108
increases upon the protein fibrillization. Resonance energy transfer measurements suggested the possibility of direct complexation between hemoglobin and aggregated lysozyme. Using the novel squaraine dye SQ-1 it was demonstrated that aggregated lysozyme is capable of inhibiting lipid peroxidation processes. Fluorescent probes pyrene, Prodan and diphenylhexatriene were employed to characterize the membrane-modifying properties of hemoglobin and lysozyme. Both oligomeric and fibrillar forms of lysozyme were found to exert condensing influence on lipid bilayer structure, with the membrane effects of fibrils being less amenable to modulation by hemoglobin. |
| doi_str_mv | 10.1007/s10895-013-1254-2 |
| format | Article |
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62
and Trp
108
increases upon the protein fibrillization. Resonance energy transfer measurements suggested the possibility of direct complexation between hemoglobin and aggregated lysozyme. Using the novel squaraine dye SQ-1 it was demonstrated that aggregated lysozyme is capable of inhibiting lipid peroxidation processes. Fluorescent probes pyrene, Prodan and diphenylhexatriene were employed to characterize the membrane-modifying properties of hemoglobin and lysozyme. Both oligomeric and fibrillar forms of lysozyme were found to exert condensing influence on lipid bilayer structure, with the membrane effects of fibrils being less amenable to modulation by hemoglobin.</description><identifier>ISSN: 1053-0509</identifier><identifier>EISSN: 1573-4994</identifier><identifier>DOI: 10.1007/s10895-013-1254-2</identifier><identifier>PMID: 23807458</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Acrylamide - chemical synthesis ; Acrylamide - chemistry ; Acrylamide - metabolism ; Amyloid - chemical synthesis ; Amyloid - chemistry ; Amyloid - metabolism ; Analytical Chemistry ; Animals ; Biochemistry ; Biological and Medical Physics ; Biomedical and Life Sciences ; Biomedicine ; Biophysics ; Biotechnology ; Chickens ; Egg White - chemistry ; Erythrocytes ; Fluorescence ; Fluorescent Dyes - chemical synthesis ; Fluorescent Dyes - chemistry ; Fluorescent Dyes - metabolism ; Hemoglobin ; Hemoglobins - chemistry ; Hemoglobins - metabolism ; Lipid Bilayers - chemistry ; Lipid Bilayers - metabolism ; Lipids ; Liposomes - chemistry ; Liposomes - metabolism ; Lysozyme ; Membranes ; Muramidase - chemistry ; Muramidase - metabolism ; Original Paper ; Proteins ; Spectrometry, Fluorescence ; Toxicity</subject><ispartof>Journal of fluorescence, 2013-11, Vol.23 (6), p.1229-1237</ispartof><rights>Springer Science+Business Media New York 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c377t-9537cc1be8ffc3a68f46cd1bf3ac60498666a7af904c8fc254fed7aebe0acb633</citedby><cites>FETCH-LOGICAL-c377t-9537cc1be8ffc3a68f46cd1bf3ac60498666a7af904c8fc254fed7aebe0acb633</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10895-013-1254-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10895-013-1254-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23807458$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kutsenko, Olga K.</creatorcontrib><creatorcontrib>Trusova, Valeriya M.</creatorcontrib><creatorcontrib>Gorbenko, Galyna P.</creatorcontrib><creatorcontrib>Lipovaya, Anna S.</creatorcontrib><creatorcontrib>Slobozhanina, Ekaterina I.</creatorcontrib><creatorcontrib>Lukyanenko, Lyudmila M.</creatorcontrib><creatorcontrib>Deligeorgiev, Todor</creatorcontrib><creatorcontrib>Vasilev, Aleksey</creatorcontrib><title>Fluorescence Study of the Membrane Effects of Aggregated Lysozyme</title><title>Journal of fluorescence</title><addtitle>J Fluoresc</addtitle><addtitle>J Fluoresc</addtitle><description>The last decade has seen unprecedented upsurge of interest in the structural and toxic properties of particular type of protein aggregates, amyloid fibrils, associated with a number of pathological states. In the present study fluorescence spectroscopy technique has been employed to gain further insight into the membrane-related mechanisms of amyloid toxicity. To this end, erythrocyte model system composed of liposomes and hemoglobin was subjected to the action of oligomeric and fibrillar lysozyme. Acrylamide quenching of lysozyme fluorescence showed that solvent accessibility of Trp
62
and Trp
108
increases upon the protein fibrillization. Resonance energy transfer measurements suggested the possibility of direct complexation between hemoglobin and aggregated lysozyme. Using the novel squaraine dye SQ-1 it was demonstrated that aggregated lysozyme is capable of inhibiting lipid peroxidation processes. Fluorescent probes pyrene, Prodan and diphenylhexatriene were employed to characterize the membrane-modifying properties of hemoglobin and lysozyme. Both oligomeric and fibrillar forms of lysozyme were found to exert condensing influence on lipid bilayer structure, with the membrane effects of fibrils being less amenable to modulation by hemoglobin.</description><subject>Acrylamide - chemical synthesis</subject><subject>Acrylamide - chemistry</subject><subject>Acrylamide - metabolism</subject><subject>Amyloid - chemical synthesis</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - metabolism</subject><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Biophysics</subject><subject>Biotechnology</subject><subject>Chickens</subject><subject>Egg White - chemistry</subject><subject>Erythrocytes</subject><subject>Fluorescence</subject><subject>Fluorescent Dyes - chemical synthesis</subject><subject>Fluorescent Dyes - chemistry</subject><subject>Fluorescent Dyes - metabolism</subject><subject>Hemoglobin</subject><subject>Hemoglobins - chemistry</subject><subject>Hemoglobins - metabolism</subject><subject>Lipid Bilayers - chemistry</subject><subject>Lipid Bilayers - metabolism</subject><subject>Lipids</subject><subject>Liposomes - chemistry</subject><subject>Liposomes - metabolism</subject><subject>Lysozyme</subject><subject>Membranes</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - metabolism</subject><subject>Original Paper</subject><subject>Proteins</subject><subject>Spectrometry, Fluorescence</subject><subject>Toxicity</subject><issn>1053-0509</issn><issn>1573-4994</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kD1PwzAQhi0EoqXwA1hQRpaAHcdfY1W1gFTEAMyW45xDq3wUOxnCr8dVgJHpTnfvvXrvQeia4DuCsbgPBEvFUkxoSjKWp9kJmhMmaJorlZ_GHjOaYobVDF2EsMcYK5nLczTLqMQiZ3KOlpt66DwEC62F5LUfyjHpXNJ_QPIMTeFNC8naObB9OM6XVeWhMj2UyXYM3dfYwCU6c6YOcPVTF-h9s35bPabbl4en1XKbWipEnypGhbWkAOmcpYZLl3NbksJRYznOleScG2GcwrmVzsZ3HJTCQAHY2IJTukC3k-_Bd58DhF43uxi7rmPEbgiacEEYIYyrKCWT1PouBA9OH_yuMX7UBOsjOT2R05GcPpLTWby5-bEfigbKv4tfVFGQTYIQV20FXu-7wbfx5X9cvwHkPHli</recordid><startdate>20131101</startdate><enddate>20131101</enddate><creator>Kutsenko, Olga K.</creator><creator>Trusova, Valeriya M.</creator><creator>Gorbenko, Galyna P.</creator><creator>Lipovaya, Anna S.</creator><creator>Slobozhanina, Ekaterina I.</creator><creator>Lukyanenko, Lyudmila M.</creator><creator>Deligeorgiev, Todor</creator><creator>Vasilev, Aleksey</creator><general>Springer US</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>7U5</scope><scope>8FD</scope><scope>L7M</scope></search><sort><creationdate>20131101</creationdate><title>Fluorescence Study of the Membrane Effects of Aggregated Lysozyme</title><author>Kutsenko, Olga K. ; Trusova, Valeriya M. ; Gorbenko, Galyna P. ; Lipovaya, Anna S. ; Slobozhanina, Ekaterina I. ; Lukyanenko, Lyudmila M. ; Deligeorgiev, Todor ; Vasilev, Aleksey</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c377t-9537cc1be8ffc3a68f46cd1bf3ac60498666a7af904c8fc254fed7aebe0acb633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Acrylamide - chemical synthesis</topic><topic>Acrylamide - chemistry</topic><topic>Acrylamide - metabolism</topic><topic>Amyloid - chemical synthesis</topic><topic>Amyloid - chemistry</topic><topic>Amyloid - metabolism</topic><topic>Analytical Chemistry</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Biophysics</topic><topic>Biotechnology</topic><topic>Chickens</topic><topic>Egg White - chemistry</topic><topic>Erythrocytes</topic><topic>Fluorescence</topic><topic>Fluorescent Dyes - chemical synthesis</topic><topic>Fluorescent Dyes - chemistry</topic><topic>Fluorescent Dyes - metabolism</topic><topic>Hemoglobin</topic><topic>Hemoglobins - chemistry</topic><topic>Hemoglobins - metabolism</topic><topic>Lipid Bilayers - chemistry</topic><topic>Lipid Bilayers - metabolism</topic><topic>Lipids</topic><topic>Liposomes - chemistry</topic><topic>Liposomes - metabolism</topic><topic>Lysozyme</topic><topic>Membranes</topic><topic>Muramidase - chemistry</topic><topic>Muramidase - metabolism</topic><topic>Original Paper</topic><topic>Proteins</topic><topic>Spectrometry, Fluorescence</topic><topic>Toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kutsenko, Olga K.</creatorcontrib><creatorcontrib>Trusova, Valeriya M.</creatorcontrib><creatorcontrib>Gorbenko, Galyna P.</creatorcontrib><creatorcontrib>Lipovaya, Anna S.</creatorcontrib><creatorcontrib>Slobozhanina, Ekaterina I.</creatorcontrib><creatorcontrib>Lukyanenko, Lyudmila M.</creatorcontrib><creatorcontrib>Deligeorgiev, Todor</creatorcontrib><creatorcontrib>Vasilev, Aleksey</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Journal of fluorescence</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kutsenko, Olga K.</au><au>Trusova, Valeriya M.</au><au>Gorbenko, Galyna P.</au><au>Lipovaya, Anna S.</au><au>Slobozhanina, Ekaterina I.</au><au>Lukyanenko, Lyudmila M.</au><au>Deligeorgiev, Todor</au><au>Vasilev, Aleksey</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fluorescence Study of the Membrane Effects of Aggregated Lysozyme</atitle><jtitle>Journal of fluorescence</jtitle><stitle>J Fluoresc</stitle><addtitle>J Fluoresc</addtitle><date>2013-11-01</date><risdate>2013</risdate><volume>23</volume><issue>6</issue><spage>1229</spage><epage>1237</epage><pages>1229-1237</pages><issn>1053-0509</issn><eissn>1573-4994</eissn><abstract>The last decade has seen unprecedented upsurge of interest in the structural and toxic properties of particular type of protein aggregates, amyloid fibrils, associated with a number of pathological states. In the present study fluorescence spectroscopy technique has been employed to gain further insight into the membrane-related mechanisms of amyloid toxicity. To this end, erythrocyte model system composed of liposomes and hemoglobin was subjected to the action of oligomeric and fibrillar lysozyme. Acrylamide quenching of lysozyme fluorescence showed that solvent accessibility of Trp
62
and Trp
108
increases upon the protein fibrillization. Resonance energy transfer measurements suggested the possibility of direct complexation between hemoglobin and aggregated lysozyme. Using the novel squaraine dye SQ-1 it was demonstrated that aggregated lysozyme is capable of inhibiting lipid peroxidation processes. Fluorescent probes pyrene, Prodan and diphenylhexatriene were employed to characterize the membrane-modifying properties of hemoglobin and lysozyme. Both oligomeric and fibrillar forms of lysozyme were found to exert condensing influence on lipid bilayer structure, with the membrane effects of fibrils being less amenable to modulation by hemoglobin.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>23807458</pmid><doi>10.1007/s10895-013-1254-2</doi><tpages>9</tpages></addata></record> |
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| subjects | Acrylamide - chemical synthesis Acrylamide - chemistry Acrylamide - metabolism Amyloid - chemical synthesis Amyloid - chemistry Amyloid - metabolism Analytical Chemistry Animals Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biomedicine Biophysics Biotechnology Chickens Egg White - chemistry Erythrocytes Fluorescence Fluorescent Dyes - chemical synthesis Fluorescent Dyes - chemistry Fluorescent Dyes - metabolism Hemoglobin Hemoglobins - chemistry Hemoglobins - metabolism Lipid Bilayers - chemistry Lipid Bilayers - metabolism Lipids Liposomes - chemistry Liposomes - metabolism Lysozyme Membranes Muramidase - chemistry Muramidase - metabolism Original Paper Proteins Spectrometry, Fluorescence Toxicity |
| title | Fluorescence Study of the Membrane Effects of Aggregated Lysozyme |
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