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Exploring the binding mechanisms of inorganic magnetic nanocarrier containing L-Dopa with HSA protein utilizing multi spectroscopic techniques
In this study, the interaction of Fe 3 O 4 @CaAl-LDH@L-Dopa nanoparticles (NPs) with human serum albumin (HSA) was investigated in simulated physiological conditions applying UV-visible, fluorescence, and circular dichroism (CD) spectroscopic techniques. The consequences of UV-vis and CD spectroscop...
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| Published in: | Journal of biomolecular structure & dynamics 2021-12, Vol.39 (18), p.7160-7167 |
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| Main Authors: | , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c343t-e959123406cb5be5f34c1388e3b52d3ddd3dc7505a789e8e37f066bce4de0ab83 |
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| cites | cdi_FETCH-LOGICAL-c343t-e959123406cb5be5f34c1388e3b52d3ddd3dc7505a789e8e37f066bce4de0ab83 |
| container_end_page | 7167 |
| container_issue | 18 |
| container_start_page | 7160 |
| container_title | Journal of biomolecular structure & dynamics |
| container_volume | 39 |
| creator | Shahabadi, Nahid Razlansari, Mahtab |
| description | In this study, the interaction of Fe
3
O
4
@CaAl-LDH@L-Dopa nanoparticles (NPs) with human serum albumin (HSA) was investigated in simulated physiological conditions applying UV-visible, fluorescence, and circular dichroism (CD) spectroscopic techniques. The consequences of UV-vis and CD spectroscopy demonstrated that the interaction of HSA to Fe
3
O
4
@CaAl-LDH@L-Dopa NPs enforced some conformational alterations within HSA. The fluorescence spectroscopy analysis indicated that by enhancing temperature, the Stern-Volmer quenching constant (K
sv
) was decreased, which is relevant to a static quenching mechanism. The binding constant (K
b
) was 7.07 × 10
4
M
−1
while the number of the binding site (n) was 0.94 which is in compromise with its binding constant. Also, thermodynamic parameters (ΔH° > 0, ΔG° < 0, and ΔS° > 0) have suggested that hydrophobic forces perform a key role in the interaction of HSA with Fe
3
O
4
@CaAl-LDH@L-Dopa NPs. Displacement studies successfully carried out using the Warfarin and Ibuprofen have predicted that the binding of Fe
3
O
4
@CaAl-LDH@L-Dopa NPs to HSA is situated at site II (subdomain IIIA).
Communicated by Ramaswamy H. Sarma |
| doi_str_mv | 10.1080/07391102.2020.1806929 |
| format | article |
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3
O
4
@CaAl-LDH@L-Dopa nanoparticles (NPs) with human serum albumin (HSA) was investigated in simulated physiological conditions applying UV-visible, fluorescence, and circular dichroism (CD) spectroscopic techniques. The consequences of UV-vis and CD spectroscopy demonstrated that the interaction of HSA to Fe
3
O
4
@CaAl-LDH@L-Dopa NPs enforced some conformational alterations within HSA. The fluorescence spectroscopy analysis indicated that by enhancing temperature, the Stern-Volmer quenching constant (K
sv
) was decreased, which is relevant to a static quenching mechanism. The binding constant (K
b
) was 7.07 × 10
4
M
−1
while the number of the binding site (n) was 0.94 which is in compromise with its binding constant. Also, thermodynamic parameters (ΔH° > 0, ΔG° < 0, and ΔS° > 0) have suggested that hydrophobic forces perform a key role in the interaction of HSA with Fe
3
O
4
@CaAl-LDH@L-Dopa NPs. Displacement studies successfully carried out using the Warfarin and Ibuprofen have predicted that the binding of Fe
3
O
4
@CaAl-LDH@L-Dopa NPs to HSA is situated at site II (subdomain IIIA).
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3
O
4
@CaAl-LDH@L-Dopa nanoparticles (NPs) with human serum albumin (HSA) was investigated in simulated physiological conditions applying UV-visible, fluorescence, and circular dichroism (CD) spectroscopic techniques. The consequences of UV-vis and CD spectroscopy demonstrated that the interaction of HSA to Fe
3
O
4
@CaAl-LDH@L-Dopa NPs enforced some conformational alterations within HSA. The fluorescence spectroscopy analysis indicated that by enhancing temperature, the Stern-Volmer quenching constant (K
sv
) was decreased, which is relevant to a static quenching mechanism. The binding constant (K
b
) was 7.07 × 10
4
M
−1
while the number of the binding site (n) was 0.94 which is in compromise with its binding constant. Also, thermodynamic parameters (ΔH° > 0, ΔG° < 0, and ΔS° > 0) have suggested that hydrophobic forces perform a key role in the interaction of HSA with Fe
3
O
4
@CaAl-LDH@L-Dopa NPs. Displacement studies successfully carried out using the Warfarin and Ibuprofen have predicted that the binding of Fe
3
O
4
@CaAl-LDH@L-Dopa NPs to HSA is situated at site II (subdomain IIIA).
Communicated by Ramaswamy H. Sarma</description><subject>binding constant</subject><subject>HSA</subject><subject>L-Dopa</subject><subject>Multi spectroscopy</subject><issn>0739-1102</issn><issn>1538-0254</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp9kMtOwzAQRS0EEuXxCUhesknxI26SHagUilSJBbC2HGfSGiV2sF0V-Ai-GYfCloXlmdG9d0YHoQtKppSU5IoUvKKUsCkjLI1KMqtYdYAmVPAyI0zkh2gyarJRdIxOQnglhFFa0An6WrwPnfPGrnHcAK6Nbca6B71R1oQ-YNdiY51fp1bjXq0txFRYZZ1W3hvwWDsblbGjb5XdukHhnYkbvHy6wYN3EYzF22g68_mTvO2iwWEAHb0L2g0pLKZt1rxtIZyho1Z1Ac5__1P0crd4ni-z1eP9w_xmlWme85hBJSrKeE5muhY1iJbnmvKyBF4L1vCmSU8XgghVlBWkcdGS2azWkDdAVF3yU3S5z00Hjnuj7E3Q0HXKgtsGyXKe5wUtCE9SsZfqdG_w0MrBm175D0mJHPnLP_5y5C9_-Sff9d5nbOt8r3bOd42M6iPhbr2y2gTJ_4_4Bo6wkDY</recordid><startdate>20211212</startdate><enddate>20211212</enddate><creator>Shahabadi, Nahid</creator><creator>Razlansari, Mahtab</creator><general>Taylor & Francis</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20211212</creationdate><title>Exploring the binding mechanisms of inorganic magnetic nanocarrier containing L-Dopa with HSA protein utilizing multi spectroscopic techniques</title><author>Shahabadi, Nahid ; Razlansari, Mahtab</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c343t-e959123406cb5be5f34c1388e3b52d3ddd3dc7505a789e8e37f066bce4de0ab83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>binding constant</topic><topic>HSA</topic><topic>L-Dopa</topic><topic>Multi spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shahabadi, Nahid</creatorcontrib><creatorcontrib>Razlansari, Mahtab</creatorcontrib><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biomolecular structure & dynamics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shahabadi, Nahid</au><au>Razlansari, Mahtab</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Exploring the binding mechanisms of inorganic magnetic nanocarrier containing L-Dopa with HSA protein utilizing multi spectroscopic techniques</atitle><jtitle>Journal of biomolecular structure & dynamics</jtitle><date>2021-12-12</date><risdate>2021</risdate><volume>39</volume><issue>18</issue><spage>7160</spage><epage>7167</epage><pages>7160-7167</pages><issn>0739-1102</issn><eissn>1538-0254</eissn><abstract>In this study, the interaction of Fe
3
O
4
@CaAl-LDH@L-Dopa nanoparticles (NPs) with human serum albumin (HSA) was investigated in simulated physiological conditions applying UV-visible, fluorescence, and circular dichroism (CD) spectroscopic techniques. The consequences of UV-vis and CD spectroscopy demonstrated that the interaction of HSA to Fe
3
O
4
@CaAl-LDH@L-Dopa NPs enforced some conformational alterations within HSA. The fluorescence spectroscopy analysis indicated that by enhancing temperature, the Stern-Volmer quenching constant (K
sv
) was decreased, which is relevant to a static quenching mechanism. The binding constant (K
b
) was 7.07 × 10
4
M
−1
while the number of the binding site (n) was 0.94 which is in compromise with its binding constant. Also, thermodynamic parameters (ΔH° > 0, ΔG° < 0, and ΔS° > 0) have suggested that hydrophobic forces perform a key role in the interaction of HSA with Fe
3
O
4
@CaAl-LDH@L-Dopa NPs. Displacement studies successfully carried out using the Warfarin and Ibuprofen have predicted that the binding of Fe
3
O
4
@CaAl-LDH@L-Dopa NPs to HSA is situated at site II (subdomain IIIA).
Communicated by Ramaswamy H. Sarma</abstract><pub>Taylor & Francis</pub><doi>10.1080/07391102.2020.1806929</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 0739-1102 |
| ispartof | Journal of biomolecular structure & dynamics, 2021-12, Vol.39 (18), p.7160-7167 |
| issn | 0739-1102 1538-0254 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2434471703 |
| source | Taylor and Francis Science and Technology Collection |
| subjects | binding constant HSA L-Dopa Multi spectroscopy |
| title | Exploring the binding mechanisms of inorganic magnetic nanocarrier containing L-Dopa with HSA protein utilizing multi spectroscopic techniques |
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