Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques
The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect thi...
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description | The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated. |
doi_str_mv | 10.3390/ma14020298 |
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Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.</description><identifier>ISSN: 1996-1944</identifier><identifier>EISSN: 1996-1944</identifier><identifier>DOI: 10.3390/ma14020298</identifier><identifier>PMID: 33430090</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Binding sites ; Experiments ; Fluorescence ; Light ; Morphology ; Nanomaterials ; Nanoparticles ; Particle size ; Proteins ; Research methodology ; Serum albumin</subject><ispartof>Materials, 2021-01, Vol.14 (2), p.298</ispartof><rights>2021. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 by the authors. 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2988-a25df1ccf80ad45ce9dd4cb7640f8f99d01e3cf42adada370df7cb74a39ed2803</citedby><cites>FETCH-LOGICAL-c2988-a25df1ccf80ad45ce9dd4cb7640f8f99d01e3cf42adada370df7cb74a39ed2803</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7827174/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7827174/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids></links><search><creatorcontrib>Liu, Shufang</creatorcontrib><creatorcontrib>Wang, Shu’e</creatorcontrib><creatorcontrib>Liu, Zhanzuo</creatorcontrib><title>Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques</title><title>Materials</title><description>The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.</description><subject>Binding sites</subject><subject>Experiments</subject><subject>Fluorescence</subject><subject>Light</subject><subject>Morphology</subject><subject>Nanomaterials</subject><subject>Nanoparticles</subject><subject>Particle size</subject><subject>Proteins</subject><subject>Research methodology</subject><subject>Serum albumin</subject><issn>1996-1944</issn><issn>1996-1944</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNpdkV9LHDEUxYMoVdQXP0HAFymMzT9nJi-CblsrWFpYfQ7Z5GY3MpNMk5kF--mbqdKqyUNuOD8O99yL0Akl55xL8qnXVBBGmGx30AGVsq6oFGL3Vb2PjnN-JOVwTlsmP6B9zgUnRJIDlG_DFvLo13r0YY3HDeCl_w3VZxggWAgjvvbBzlJ0-GfyBQ2Aw6ImeIz4Om7n7xLS1OOrbjX1PuDVE_4-daOvlgOYMcVs4uANvgezCf7XBPkI7TndZTh-eQ_Rw9cv94tv1d2Pm9vF1V1lSpq20uzCOmqMa4m24sKAtFaYVVML4lonpSUUuHGCaVsub4h1TZGF5hIsawk_RJfPvsO06sGakibpTg3J9zo9qai9eqsEv1HruFVNyxraiGJw9mKQ4tz4qHqfDXSdDhCnrJhoGlaztuYFPX2HPsYphRLvL8Vlmf1MfXymTBlLTuD-NUOJmtep_q-T_wEnO5LD</recordid><startdate>20210108</startdate><enddate>20210108</enddate><creator>Liu, Shufang</creator><creator>Wang, Shu’e</creator><creator>Liu, Zhanzuo</creator><general>MDPI AG</general><general>MDPI</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>KB.</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20210108</creationdate><title>Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques</title><author>Liu, Shufang ; Wang, Shu’e ; Liu, Zhanzuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2988-a25df1ccf80ad45ce9dd4cb7640f8f99d01e3cf42adada370df7cb74a39ed2803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Binding sites</topic><topic>Experiments</topic><topic>Fluorescence</topic><topic>Light</topic><topic>Morphology</topic><topic>Nanomaterials</topic><topic>Nanoparticles</topic><topic>Particle size</topic><topic>Proteins</topic><topic>Research methodology</topic><topic>Serum albumin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Shufang</creatorcontrib><creatorcontrib>Wang, Shu’e</creatorcontrib><creatorcontrib>Liu, Zhanzuo</creatorcontrib><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>Materials Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Materials</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Shufang</au><au>Wang, Shu’e</au><au>Liu, Zhanzuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques</atitle><jtitle>Materials</jtitle><date>2021-01-08</date><risdate>2021</risdate><volume>14</volume><issue>2</issue><spage>298</spage><pages>298-</pages><issn>1996-1944</issn><eissn>1996-1944</eissn><abstract>The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.</abstract><cop>Basel</cop><pub>MDPI AG</pub><pmid>33430090</pmid><doi>10.3390/ma14020298</doi><oa>free_for_read</oa></addata></record> |
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subjects | Binding sites Experiments Fluorescence Light Morphology Nanomaterials Nanoparticles Particle size Proteins Research methodology Serum albumin |
title | Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques |
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