Molecular Interaction of Functionalized Nanoplastics with Human Hemoglobin
Humans are exposed to excessive nanoplastics (NPs) which have ample affinity for globular proteins. We investigated the interaction of functionalized polystyrene nanoplastics (plain: PS, carboxy: PS-COOH, and amine: PS-NH 2 ) with human hemoglobin (Hb) utilizing multi-spectroscopic and docking appro...
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| Veröffentlicht in: | Journal of fluorescence 2023-11, Vol.33 (6), p.2257-2272 |
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| creator | Rajendran, Durgalakshmi Chandrasekaran, Natarajan |
| description | Humans are exposed to excessive nanoplastics (NPs) which have ample affinity for globular proteins. We investigated the interaction of functionalized polystyrene nanoplastics (plain: PS, carboxy: PS-COOH, and amine: PS-NH
2
) with human hemoglobin (Hb) utilizing multi-spectroscopic and docking approaches to acquire insights into molecular aspects of binding mechanism, which will be helpful in assessing the toxicokinetics or toxicodynamics of nanoplastics NPs. Hypsochromicity and hypochromicity were observed invariably in all the spectra (steady-state fluorescence emission, synchronous and three-dimensional) for all complexes, among which PS-NH
2
binds effectively and changes the Hb’s conformation by enhancing hydrophobicity around aromatic residues, notably tryptophan. All the NPs bind with the hydrophobic pocket of B-chain in Hb, where PS and PS-NH
2
bind via hydrophobic force while PS-COOH binds via hydrogen bonding (predominantly) and van der Waals force, consistent validated with docking results. The minimal shift in absorbance peak also indicates enhanced hydrophobicity by PS-NH
2
with larger aggregation as demonstrated in resonance light scattering. The amide band’s shift, secondary structural analysis, and presence of characteristic functional group peaks in complexes in Infra-Red spectra confirm the structural changes in the protein. As seen in field emission scanning microscopy images, NPs penetrate the surface of proteins. These findings conclude that polystyrene NPs interact with Hb, causing structural alterations that may affect functional characteristics as well, with the greatest effect being in the order: PS-NH
2
>PS-COOH>PS.
Graphical Abstract |
| doi_str_mv | 10.1007/s10895-023-03221-3 |
| format | Article |
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2
) with human hemoglobin (Hb) utilizing multi-spectroscopic and docking approaches to acquire insights into molecular aspects of binding mechanism, which will be helpful in assessing the toxicokinetics or toxicodynamics of nanoplastics NPs. Hypsochromicity and hypochromicity were observed invariably in all the spectra (steady-state fluorescence emission, synchronous and three-dimensional) for all complexes, among which PS-NH
2
binds effectively and changes the Hb’s conformation by enhancing hydrophobicity around aromatic residues, notably tryptophan. All the NPs bind with the hydrophobic pocket of B-chain in Hb, where PS and PS-NH
2
bind via hydrophobic force while PS-COOH binds via hydrogen bonding (predominantly) and van der Waals force, consistent validated with docking results. The minimal shift in absorbance peak also indicates enhanced hydrophobicity by PS-NH
2
with larger aggregation as demonstrated in resonance light scattering. The amide band’s shift, secondary structural analysis, and presence of characteristic functional group peaks in complexes in Infra-Red spectra confirm the structural changes in the protein. As seen in field emission scanning microscopy images, NPs penetrate the surface of proteins. These findings conclude that polystyrene NPs interact with Hb, causing structural alterations that may affect functional characteristics as well, with the greatest effect being in the order: PS-NH
2
>PS-COOH>PS.
Graphical Abstract</description><identifier>ISSN: 1053-0509</identifier><identifier>EISSN: 1573-4994</identifier><identifier>DOI: 10.1007/s10895-023-03221-3</identifier><identifier>PMID: 37014521</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Analytical Chemistry ; Biochemistry ; Biological and Medical Physics ; Biomedical and Life Sciences ; Biomedicine ; Biophysics ; Biotechnology ; Docking ; Emission spectra ; Field emission microscopy ; Functional groups ; Hemoglobin ; Hydrogen bonding ; Hydrophobicity ; Molecular interactions ; Plastic pollution ; Polystyrene resins ; Proteins ; Resonance scattering ; Scanning microscopy ; Structural analysis ; Tryptophan ; Van der Waals forces</subject><ispartof>Journal of fluorescence, 2023-11, Vol.33 (6), p.2257-2272</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-de8bef2f1fd0382b149bd3e8dc4e4d98ae9533e2cd5dc5982dc8ee120fd114843</citedby><cites>FETCH-LOGICAL-c375t-de8bef2f1fd0382b149bd3e8dc4e4d98ae9533e2cd5dc5982dc8ee120fd114843</cites><orcidid>0000-0002-0586-134X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10895-023-03221-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10895-023-03221-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27915,27916,41479,42548,51310</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37014521$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rajendran, Durgalakshmi</creatorcontrib><creatorcontrib>Chandrasekaran, Natarajan</creatorcontrib><title>Molecular Interaction of Functionalized Nanoplastics with Human Hemoglobin</title><title>Journal of fluorescence</title><addtitle>J Fluoresc</addtitle><addtitle>J Fluoresc</addtitle><description>Humans are exposed to excessive nanoplastics (NPs) which have ample affinity for globular proteins. We investigated the interaction of functionalized polystyrene nanoplastics (plain: PS, carboxy: PS-COOH, and amine: PS-NH
2
) with human hemoglobin (Hb) utilizing multi-spectroscopic and docking approaches to acquire insights into molecular aspects of binding mechanism, which will be helpful in assessing the toxicokinetics or toxicodynamics of nanoplastics NPs. Hypsochromicity and hypochromicity were observed invariably in all the spectra (steady-state fluorescence emission, synchronous and three-dimensional) for all complexes, among which PS-NH
2
binds effectively and changes the Hb’s conformation by enhancing hydrophobicity around aromatic residues, notably tryptophan. All the NPs bind with the hydrophobic pocket of B-chain in Hb, where PS and PS-NH
2
bind via hydrophobic force while PS-COOH binds via hydrogen bonding (predominantly) and van der Waals force, consistent validated with docking results. The minimal shift in absorbance peak also indicates enhanced hydrophobicity by PS-NH
2
with larger aggregation as demonstrated in resonance light scattering. The amide band’s shift, secondary structural analysis, and presence of characteristic functional group peaks in complexes in Infra-Red spectra confirm the structural changes in the protein. As seen in field emission scanning microscopy images, NPs penetrate the surface of proteins. These findings conclude that polystyrene NPs interact with Hb, causing structural alterations that may affect functional characteristics as well, with the greatest effect being in the order: PS-NH
2
>PS-COOH>PS.
Graphical Abstract</description><subject>Analytical Chemistry</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>Docking</subject><subject>Emission spectra</subject><subject>Field emission microscopy</subject><subject>Functional groups</subject><subject>Hemoglobin</subject><subject>Hydrogen bonding</subject><subject>Hydrophobicity</subject><subject>Molecular interactions</subject><subject>Plastic pollution</subject><subject>Polystyrene resins</subject><subject>Proteins</subject><subject>Resonance scattering</subject><subject>Scanning microscopy</subject><subject>Structural analysis</subject><subject>Tryptophan</subject><subject>Van der Waals forces</subject><issn>1053-0509</issn><issn>1573-4994</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp9kMtKxTAQhoMo3l_AhRTcuKlObjRZiqjniJeNrkOaTLXSNsekRfTpjR4v4MLVDMw3_zAfIXsUjihAdZwoKC1LYLwEzhgt-QrZpLLipdBarOYeZB5J0BtkK6UnANBKqHWywSugQjK6SS6vQ4du6mws5sOI0bqxDUMRmuJ8Gj5727Vv6IsbO4RFZ9PYulS8tONjMZt6OxQz7MNDF-p22CFrje0S7n7VbXJ_fnZ3Oiuvbi_mpydXpeOVHEuPqsaGNbTxwBWrqdC156i8Eyi8Vha15ByZ89I7qRXzTiFSBo2nVCjBt8nhMncRw_OEaTR9mxx2nR0wTMmwKgdIBVxn9OAP-hSmmF_KlFI6SwTGMsWWlIshpYiNWcS2t_HVUDAfps3StMmmzadpw_PS_lf0VPfof1a-1WaAL4GUR8MDxt_b_8S-A-KsiVE</recordid><startdate>20231101</startdate><enddate>20231101</enddate><creator>Rajendran, Durgalakshmi</creator><creator>Chandrasekaran, Natarajan</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-0586-134X</orcidid></search><sort><creationdate>20231101</creationdate><title>Molecular Interaction of Functionalized Nanoplastics with Human Hemoglobin</title><author>Rajendran, Durgalakshmi ; Chandrasekaran, Natarajan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-de8bef2f1fd0382b149bd3e8dc4e4d98ae9533e2cd5dc5982dc8ee120fd114843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Analytical Chemistry</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>Docking</topic><topic>Emission spectra</topic><topic>Field emission microscopy</topic><topic>Functional groups</topic><topic>Hemoglobin</topic><topic>Hydrogen bonding</topic><topic>Hydrophobicity</topic><topic>Molecular interactions</topic><topic>Plastic pollution</topic><topic>Polystyrene resins</topic><topic>Proteins</topic><topic>Resonance scattering</topic><topic>Scanning microscopy</topic><topic>Structural analysis</topic><topic>Tryptophan</topic><topic>Van der Waals forces</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rajendran, Durgalakshmi</creatorcontrib><creatorcontrib>Chandrasekaran, Natarajan</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of fluorescence</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rajendran, Durgalakshmi</au><au>Chandrasekaran, Natarajan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Interaction of Functionalized Nanoplastics with Human Hemoglobin</atitle><jtitle>Journal of fluorescence</jtitle><stitle>J Fluoresc</stitle><addtitle>J Fluoresc</addtitle><date>2023-11-01</date><risdate>2023</risdate><volume>33</volume><issue>6</issue><spage>2257</spage><epage>2272</epage><pages>2257-2272</pages><issn>1053-0509</issn><eissn>1573-4994</eissn><abstract>Humans are exposed to excessive nanoplastics (NPs) which have ample affinity for globular proteins. We investigated the interaction of functionalized polystyrene nanoplastics (plain: PS, carboxy: PS-COOH, and amine: PS-NH
2
) with human hemoglobin (Hb) utilizing multi-spectroscopic and docking approaches to acquire insights into molecular aspects of binding mechanism, which will be helpful in assessing the toxicokinetics or toxicodynamics of nanoplastics NPs. Hypsochromicity and hypochromicity were observed invariably in all the spectra (steady-state fluorescence emission, synchronous and three-dimensional) for all complexes, among which PS-NH
2
binds effectively and changes the Hb’s conformation by enhancing hydrophobicity around aromatic residues, notably tryptophan. All the NPs bind with the hydrophobic pocket of B-chain in Hb, where PS and PS-NH
2
bind via hydrophobic force while PS-COOH binds via hydrogen bonding (predominantly) and van der Waals force, consistent validated with docking results. The minimal shift in absorbance peak also indicates enhanced hydrophobicity by PS-NH
2
with larger aggregation as demonstrated in resonance light scattering. The amide band’s shift, secondary structural analysis, and presence of characteristic functional group peaks in complexes in Infra-Red spectra confirm the structural changes in the protein. As seen in field emission scanning microscopy images, NPs penetrate the surface of proteins. These findings conclude that polystyrene NPs interact with Hb, causing structural alterations that may affect functional characteristics as well, with the greatest effect being in the order: PS-NH
2
>PS-COOH>PS.
Graphical Abstract</abstract><cop>New York</cop><pub>Springer US</pub><pmid>37014521</pmid><doi>10.1007/s10895-023-03221-3</doi><tpages>16</tpages><orcidid>https://orcid.org/0000-0002-0586-134X</orcidid></addata></record> |
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| subjects | Analytical Chemistry Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biomedicine Biophysics Biotechnology Docking Emission spectra Field emission microscopy Functional groups Hemoglobin Hydrogen bonding Hydrophobicity Molecular interactions Plastic pollution Polystyrene resins Proteins Resonance scattering Scanning microscopy Structural analysis Tryptophan Van der Waals forces |
| title | Molecular Interaction of Functionalized Nanoplastics with Human Hemoglobin |
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