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Construing the interactions between MnO 2 nanoparticle and bovine serum albumin: insight into the structure and stability of a protein–nanoparticle complex
A systematic study of the interaction of bovine serum albumin (BSA) with MnO 2 nanoparticles (NPs) was carried out. MnO 2 nanoparticles were prepared via a low temperature (90 °C) single-step precipitation route in the absence of surfactant/template and characterized using XRD, TEM, FESEM, FTIR, XPS...
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Published in: | New journal of chemistry 2017, Vol.41 (16), p.8130-8139 |
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container_end_page | 8139 |
container_issue | 16 |
container_start_page | 8130 |
container_title | New journal of chemistry |
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creator | Baral, Ayonbala Satish, Lakkoji Das, Dipti P. Sahoo, Harekrushna Ghosh, Malay K. |
description | A systematic study of the interaction of bovine serum albumin (BSA) with MnO
2
nanoparticles (NPs) was carried out. MnO
2
nanoparticles were prepared
via
a low temperature (90 °C) single-step precipitation route in the absence of surfactant/template and characterized using XRD, TEM, FESEM, FTIR, XPS, and Raman spectroscopy. MnO
2
particles were found to have a length of 900 nm and a diameter of 10 nm. The interaction of BSA with NP was investigated using various spectroscopic and biophysical techniques under physiological pH 7.4. MnO
2
effectively quenches the intrinsic fluorescence of BSA through static quenching. The effect of MnO
2
on the conformation of BSA was analyzed using circular dichroism (CD), Fourier transform infrared (FTIR), and Raman spectroscopy, and it was observed that the secondary structure of BSA altered after the interaction with MnO
2
. Thermal CD spectroscopy revealed insignificant variation in the melting temperature of BSA upon binding to MnO
2
. Additionally, the morphological changes of BSA upon interaction with MnO
2
were characterized using a field emission scanning electron microscope (FESEM). Moreover, the increase in the size of the BSA–MnO
2
complexes was analyzed using dynamic light scattering (DLS). This study shows that the adsorption of BSA on MnO
2
is dependent on the concentration of the protein as well as the NP. |
doi_str_mv | 10.1039/C7NJ01227F |
format | article |
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2
nanoparticles (NPs) was carried out. MnO
2
nanoparticles were prepared
via
a low temperature (90 °C) single-step precipitation route in the absence of surfactant/template and characterized using XRD, TEM, FESEM, FTIR, XPS, and Raman spectroscopy. MnO
2
particles were found to have a length of 900 nm and a diameter of 10 nm. The interaction of BSA with NP was investigated using various spectroscopic and biophysical techniques under physiological pH 7.4. MnO
2
effectively quenches the intrinsic fluorescence of BSA through static quenching. The effect of MnO
2
on the conformation of BSA was analyzed using circular dichroism (CD), Fourier transform infrared (FTIR), and Raman spectroscopy, and it was observed that the secondary structure of BSA altered after the interaction with MnO
2
. Thermal CD spectroscopy revealed insignificant variation in the melting temperature of BSA upon binding to MnO
2
. Additionally, the morphological changes of BSA upon interaction with MnO
2
were characterized using a field emission scanning electron microscope (FESEM). Moreover, the increase in the size of the BSA–MnO
2
complexes was analyzed using dynamic light scattering (DLS). This study shows that the adsorption of BSA on MnO
2
is dependent on the concentration of the protein as well as the NP.</description><identifier>ISSN: 1144-0546</identifier><identifier>EISSN: 1369-9261</identifier><identifier>DOI: 10.1039/C7NJ01227F</identifier><language>eng</language><ispartof>New journal of chemistry, 2017, Vol.41 (16), p.8130-8139</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c76F-c33ad34429ba1071ce2d52e7da5e88c80f34fe72e484a7f187dc567eee45fd9c3</citedby><cites>FETCH-LOGICAL-c76F-c33ad34429ba1071ce2d52e7da5e88c80f34fe72e484a7f187dc567eee45fd9c3</cites><orcidid>0000-0003-2655-1196</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,4043,27956,27957,27958</link.rule.ids></links><search><creatorcontrib>Baral, Ayonbala</creatorcontrib><creatorcontrib>Satish, Lakkoji</creatorcontrib><creatorcontrib>Das, Dipti P.</creatorcontrib><creatorcontrib>Sahoo, Harekrushna</creatorcontrib><creatorcontrib>Ghosh, Malay K.</creatorcontrib><title>Construing the interactions between MnO 2 nanoparticle and bovine serum albumin: insight into the structure and stability of a protein–nanoparticle complex</title><title>New journal of chemistry</title><description>A systematic study of the interaction of bovine serum albumin (BSA) with MnO
2
nanoparticles (NPs) was carried out. MnO
2
nanoparticles were prepared
via
a low temperature (90 °C) single-step precipitation route in the absence of surfactant/template and characterized using XRD, TEM, FESEM, FTIR, XPS, and Raman spectroscopy. MnO
2
particles were found to have a length of 900 nm and a diameter of 10 nm. The interaction of BSA with NP was investigated using various spectroscopic and biophysical techniques under physiological pH 7.4. MnO
2
effectively quenches the intrinsic fluorescence of BSA through static quenching. The effect of MnO
2
on the conformation of BSA was analyzed using circular dichroism (CD), Fourier transform infrared (FTIR), and Raman spectroscopy, and it was observed that the secondary structure of BSA altered after the interaction with MnO
2
. Thermal CD spectroscopy revealed insignificant variation in the melting temperature of BSA upon binding to MnO
2
. Additionally, the morphological changes of BSA upon interaction with MnO
2
were characterized using a field emission scanning electron microscope (FESEM). Moreover, the increase in the size of the BSA–MnO
2
complexes was analyzed using dynamic light scattering (DLS). This study shows that the adsorption of BSA on MnO
2
is dependent on the concentration of the protein as well as the NP.</description><issn>1144-0546</issn><issn>1369-9261</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNpV0L1OwzAUBWALgUQpLDyBZ6SA_xInbCii_KjQpXvkODetUWJHtgN04x2YeTmehBaQENO5OtL9hoPQKSXnlPDiopSP94QyJmd7aEJ5ViQFy-j-9qZCJCQV2SE6CuGJEEplRifoo3Q2RD8au8JxDdjYCF7paLY1riG-AFj8YBeYYausG5SPRneAlW1w7Z6NBRzAjz1WXT32xl5uhWBW67iT3De543Uc_c9TiKo2nYkb7Fqs8OBdBGM_397_8dr1Qwevx-igVV2Ak9-couXselneJvPFzV15NU-0zGaJ5lw1XAhW1IoSSTWwJmUgG5VCnuuctFy0IBmIXCjZ0lw2Os0kAIi0bQrNp-jsh9XeheChrQZveuU3FSXVbtfqb1f-BSNycJ0</recordid><startdate>2017</startdate><enddate>2017</enddate><creator>Baral, Ayonbala</creator><creator>Satish, Lakkoji</creator><creator>Das, Dipti P.</creator><creator>Sahoo, Harekrushna</creator><creator>Ghosh, Malay K.</creator><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0003-2655-1196</orcidid></search><sort><creationdate>2017</creationdate><title>Construing the interactions between MnO 2 nanoparticle and bovine serum albumin: insight into the structure and stability of a protein–nanoparticle complex</title><author>Baral, Ayonbala ; Satish, Lakkoji ; Das, Dipti P. ; Sahoo, Harekrushna ; Ghosh, Malay K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c76F-c33ad34429ba1071ce2d52e7da5e88c80f34fe72e484a7f187dc567eee45fd9c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Baral, Ayonbala</creatorcontrib><creatorcontrib>Satish, Lakkoji</creatorcontrib><creatorcontrib>Das, Dipti P.</creatorcontrib><creatorcontrib>Sahoo, Harekrushna</creatorcontrib><creatorcontrib>Ghosh, Malay K.</creatorcontrib><collection>CrossRef</collection><jtitle>New journal of chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Baral, Ayonbala</au><au>Satish, Lakkoji</au><au>Das, Dipti P.</au><au>Sahoo, Harekrushna</au><au>Ghosh, Malay K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Construing the interactions between MnO 2 nanoparticle and bovine serum albumin: insight into the structure and stability of a protein–nanoparticle complex</atitle><jtitle>New journal of chemistry</jtitle><date>2017</date><risdate>2017</risdate><volume>41</volume><issue>16</issue><spage>8130</spage><epage>8139</epage><pages>8130-8139</pages><issn>1144-0546</issn><eissn>1369-9261</eissn><abstract>A systematic study of the interaction of bovine serum albumin (BSA) with MnO
2
nanoparticles (NPs) was carried out. MnO
2
nanoparticles were prepared
via
a low temperature (90 °C) single-step precipitation route in the absence of surfactant/template and characterized using XRD, TEM, FESEM, FTIR, XPS, and Raman spectroscopy. MnO
2
particles were found to have a length of 900 nm and a diameter of 10 nm. The interaction of BSA with NP was investigated using various spectroscopic and biophysical techniques under physiological pH 7.4. MnO
2
effectively quenches the intrinsic fluorescence of BSA through static quenching. The effect of MnO
2
on the conformation of BSA was analyzed using circular dichroism (CD), Fourier transform infrared (FTIR), and Raman spectroscopy, and it was observed that the secondary structure of BSA altered after the interaction with MnO
2
. Thermal CD spectroscopy revealed insignificant variation in the melting temperature of BSA upon binding to MnO
2
. Additionally, the morphological changes of BSA upon interaction with MnO
2
were characterized using a field emission scanning electron microscope (FESEM). Moreover, the increase in the size of the BSA–MnO
2
complexes was analyzed using dynamic light scattering (DLS). This study shows that the adsorption of BSA on MnO
2
is dependent on the concentration of the protein as well as the NP.</abstract><doi>10.1039/C7NJ01227F</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-2655-1196</orcidid></addata></record> |
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source | Royal Society of Chemistry:Jisc Collections:Royal Society of Chemistry Read and Publish 2022-2024 (reading list) |
title | Construing the interactions between MnO 2 nanoparticle and bovine serum albumin: insight into the structure and stability of a protein–nanoparticle complex |
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