Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach
ABSTRACT Interaction of pendimethalin (PM) herbicide with the major transporter in human circulation, human serum albumin (HSA), was studied using fluorescence, circular dichroism (CD), and molecular modeling methods. The attenuation of the fluorescence intensity of HSA in the presence of PM reveale...
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| Veröffentlicht in: | Journal of biochemical and molecular toxicology 2017-02, Vol.31 (2), p.N/A |
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| creator | Lee, Wei Qi Affandi, Ida Syazwani M. Feroz, Shevin R. Mohamad, Saharuddin B. Tayyab, Saad |
| description | ABSTRACT
Interaction of pendimethalin (PM) herbicide with the major transporter in human circulation, human serum albumin (HSA), was studied using fluorescence, circular dichroism (CD), and molecular modeling methods. The attenuation of the fluorescence intensity of HSA in the presence of PM revealed formation of the PM–HSA complex. Analysis of the fluorescence quenching data showed moderately strong binding affinity between PM and HSA. Both hydrophobic interactions and hydrogen bonding were suggested to stabilize the PM–HSA complex, based on thermodynamic data. Binding of PM to HSA induced perturbation in the microenvironment around the aromatic fluorophores as well as secondary and tertiary structural changes in the protein. Complexation of PM with HSA led to an increase in its thermal stability. Both site marker displacement and molecular modeling results suggested site I, located in subdomain IIA as the preferred binding site of PM on HSA. |
| doi_str_mv | 10.1002/jbt.21839 |
| format | Article |
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Interaction of pendimethalin (PM) herbicide with the major transporter in human circulation, human serum albumin (HSA), was studied using fluorescence, circular dichroism (CD), and molecular modeling methods. The attenuation of the fluorescence intensity of HSA in the presence of PM revealed formation of the PM–HSA complex. Analysis of the fluorescence quenching data showed moderately strong binding affinity between PM and HSA. Both hydrophobic interactions and hydrogen bonding were suggested to stabilize the PM–HSA complex, based on thermodynamic data. Binding of PM to HSA induced perturbation in the microenvironment around the aromatic fluorophores as well as secondary and tertiary structural changes in the protein. Complexation of PM with HSA led to an increase in its thermal stability. Both site marker displacement and molecular modeling results suggested site I, located in subdomain IIA as the preferred binding site of PM on HSA.</description><identifier>ISSN: 1095-6670</identifier><identifier>EISSN: 1099-0461</identifier><identifier>DOI: 10.1002/jbt.21839</identifier><identifier>PMID: 27636401</identifier><identifier>CODEN: JBMTFQ</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>Aniline Compounds - metabolism ; Binding Sites ; Circular Dichroism ; fluorescence quenching ; herbicide ; human serum albumin ; Humans ; ligand–protein interaction ; Models, Molecular ; pendimethalin ; Protein Binding ; Serum Albumin - metabolism ; Spectrometry, Fluorescence</subject><ispartof>Journal of biochemical and molecular toxicology, 2017-02, Vol.31 (2), p.N/A</ispartof><rights>2016 Wiley Periodicals, Inc.</rights><rights>Copyright © 2017 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3019-50148fd94adf27826397aad57297b6fc2ca31ff779df2926c1b4ab3567066a63</citedby><cites>FETCH-LOGICAL-c3019-50148fd94adf27826397aad57297b6fc2ca31ff779df2926c1b4ab3567066a63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjbt.21839$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjbt.21839$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27636401$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Wei Qi</creatorcontrib><creatorcontrib>Affandi, Ida Syazwani M.</creatorcontrib><creatorcontrib>Feroz, Shevin R.</creatorcontrib><creatorcontrib>Mohamad, Saharuddin B.</creatorcontrib><creatorcontrib>Tayyab, Saad</creatorcontrib><title>Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach</title><title>Journal of biochemical and molecular toxicology</title><addtitle>J Biochem Mol Toxicol</addtitle><description>ABSTRACT
Interaction of pendimethalin (PM) herbicide with the major transporter in human circulation, human serum albumin (HSA), was studied using fluorescence, circular dichroism (CD), and molecular modeling methods. The attenuation of the fluorescence intensity of HSA in the presence of PM revealed formation of the PM–HSA complex. Analysis of the fluorescence quenching data showed moderately strong binding affinity between PM and HSA. Both hydrophobic interactions and hydrogen bonding were suggested to stabilize the PM–HSA complex, based on thermodynamic data. Binding of PM to HSA induced perturbation in the microenvironment around the aromatic fluorophores as well as secondary and tertiary structural changes in the protein. Complexation of PM with HSA led to an increase in its thermal stability. Both site marker displacement and molecular modeling results suggested site I, located in subdomain IIA as the preferred binding site of PM on HSA.</description><subject>Aniline Compounds - metabolism</subject><subject>Binding Sites</subject><subject>Circular Dichroism</subject><subject>fluorescence quenching</subject><subject>herbicide</subject><subject>human serum albumin</subject><subject>Humans</subject><subject>ligand–protein interaction</subject><subject>Models, Molecular</subject><subject>pendimethalin</subject><subject>Protein Binding</subject><subject>Serum Albumin - metabolism</subject><subject>Spectrometry, Fluorescence</subject><issn>1095-6670</issn><issn>1099-0461</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kT1vFDEQhi0EIiFQ8AeQJRooNvHHrn2mgyhAUCSa61ezXjvnkz8We50o_x5fLlAgUXmsefR4xi9Cbyk5p4Swi_20njO64eoZOqVEqY70gj5_rIdOCElO0KtS9oSQQcnhJTphUnDRE3qK7q_uwFdYXYo4WbyYOLtg1h14F_Hk2i3e4jXhXQ0QcTG5Bgx-qsHFT_g6Fne7Wwu2OQVcFqPXnIpOi9MY4oxD8kZXD7lVs_EHFSxLTqB3r9ELC76YN0_nGdp-vdpefu9ufn67vvx802lOqOoGQvuNnVUPs2VywwRXEmAeJFNyElYzDZxaK6VqfcWEplMPEx_azkKA4Gfow1HbXv1VTVnH4Io23kM0qZaRbmSzUt7zhr7_B92nmmMb7kARRgYmaKM-HindNi3Z2HHJLkB-GCkZD2GMLYzxMYzGvnsy1imY-S_55_cbcHEE7p03D_83jT--bI_K32IJlIQ</recordid><startdate>201702</startdate><enddate>201702</enddate><creator>Lee, Wei Qi</creator><creator>Affandi, Ida Syazwani M.</creator><creator>Feroz, Shevin R.</creator><creator>Mohamad, Saharuddin B.</creator><creator>Tayyab, Saad</creator><general>Wiley Subscription Services, Inc</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>7QO</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope></search><sort><creationdate>201702</creationdate><title>Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach</title><author>Lee, Wei Qi ; Affandi, Ida Syazwani M. ; Feroz, Shevin R. ; Mohamad, Saharuddin B. ; Tayyab, Saad</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3019-50148fd94adf27826397aad57297b6fc2ca31ff779df2926c1b4ab3567066a63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Aniline Compounds - metabolism</topic><topic>Binding Sites</topic><topic>Circular Dichroism</topic><topic>fluorescence quenching</topic><topic>herbicide</topic><topic>human serum albumin</topic><topic>Humans</topic><topic>ligand–protein interaction</topic><topic>Models, Molecular</topic><topic>pendimethalin</topic><topic>Protein Binding</topic><topic>Serum Albumin - metabolism</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Wei Qi</creatorcontrib><creatorcontrib>Affandi, Ida Syazwani M.</creatorcontrib><creatorcontrib>Feroz, Shevin R.</creatorcontrib><creatorcontrib>Mohamad, Saharuddin B.</creatorcontrib><creatorcontrib>Tayyab, Saad</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of biochemical and molecular toxicology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Wei Qi</au><au>Affandi, Ida Syazwani M.</au><au>Feroz, Shevin R.</au><au>Mohamad, Saharuddin B.</au><au>Tayyab, Saad</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach</atitle><jtitle>Journal of biochemical and molecular toxicology</jtitle><addtitle>J Biochem Mol Toxicol</addtitle><date>2017-02</date><risdate>2017</risdate><volume>31</volume><issue>2</issue><epage>N/A</epage><issn>1095-6670</issn><eissn>1099-0461</eissn><coden>JBMTFQ</coden><abstract>ABSTRACT
Interaction of pendimethalin (PM) herbicide with the major transporter in human circulation, human serum albumin (HSA), was studied using fluorescence, circular dichroism (CD), and molecular modeling methods. The attenuation of the fluorescence intensity of HSA in the presence of PM revealed formation of the PM–HSA complex. Analysis of the fluorescence quenching data showed moderately strong binding affinity between PM and HSA. Both hydrophobic interactions and hydrogen bonding were suggested to stabilize the PM–HSA complex, based on thermodynamic data. Binding of PM to HSA induced perturbation in the microenvironment around the aromatic fluorophores as well as secondary and tertiary structural changes in the protein. Complexation of PM with HSA led to an increase in its thermal stability. Both site marker displacement and molecular modeling results suggested site I, located in subdomain IIA as the preferred binding site of PM on HSA.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>27636401</pmid><doi>10.1002/jbt.21839</doi><tpages>9</tpages></addata></record> |
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| subjects | Aniline Compounds - metabolism Binding Sites Circular Dichroism fluorescence quenching herbicide human serum albumin Humans ligand–protein interaction Models, Molecular pendimethalin Protein Binding Serum Albumin - metabolism Spectrometry, Fluorescence |
| title | Evaluation of pendimethalin binding to human serum albumin: Insights from spectroscopic and molecular modeling approach |
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