Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations
The reverse-sequence peptides CysAlaAla and AlaAlaCys may attach to gold nanoparticles through the thiol group, and they differ primarily by whether the charged amino or the carboxylate group is proximal to the sulfur. Alanine residues in these peptides are not expected to interact significantly wit...
Gespeichert in:
| Veröffentlicht in: | The journal of physical chemistry. B 2015-09, Vol.119 (36), p.11998-12006 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 12006 |
|---|---|
| container_issue | 36 |
| container_start_page | 11998 |
| container_title | The journal of physical chemistry. B |
| container_volume | 119 |
| creator | Karki, Ichhuk Wang, Hong Geise, Natalie R Wilson, Brendan W Lewis, James P Gullion, Terry |
| description | The reverse-sequence peptides CysAlaAla and AlaAlaCys may attach to gold nanoparticles through the thiol group, and they differ primarily by whether the charged amino or the carboxylate group is proximal to the sulfur. Alanine residues in these peptides are not expected to interact significantly with the gold surface and serve to place a large separation between the amino and carboxylate groups. Solid-state NMR experiments and DFT calculations were performed to explore the structural differences between CysAlaAla on gold nanoparticles and AlaAlaCys on gold nanoparticles. It is found that the relative positions between the thiol, amino, and carboxylate groups strongly influences the structures of the peptide–gold systems. CysAlaAla orients parallel to the gold surface in a monolayer fashion, whereas AlaAlaCys forms an interdigitating bilayer-like structure that is oriented upright relative to the gold surface. |
| doi_str_mv | 10.1021/acs.jpcb.5b04299 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1770302147</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1711535298</sourcerecordid><originalsourceid>FETCH-LOGICAL-a369t-73d38e0d2bd994342b100224ebc60ca570df61ac556316ee01e74cb94f20a8af3</originalsourceid><addsrcrecordid>eNqNkc1u1DAUha2qiJbCvivkZRdk8E_iJN1VM7RFKkXqDOvIPzeSK48dbKejPgTvjNsZ2CGxsGzJ3zmy74fQOSULShj9LHVaPE5aLRpFatb3R-iUNoxUZbXHh7OgRJygdyk9EsIa1om36IQJTrq-E6fo1ybaCaZsDSQcPL4JzuB76cMkY7baQbrE6xxnnecoHV7ZcYQIXhdaQd4BeLzZBfwATxAT4DX8nPe3MuEVZIhb68Fg9YzXwVlTrbPMgO-_PWDpDV5db_BSOj07mW3w6T16M0qX4MNhP0M_rr9slrfV3febr8uru0py0eeq5YZ3QAxTpu9rXjNFy99YDUoLomXTEjMKKnXTCE4FAKHQ1lr19ciI7OTIz9DFvneKoTw45WFrkwbnpIcwp4G2LeFlwHX7HyilDW9Y3xWU7FEdQ0oRxmGKdivj80DJ8OJrKL6GF1_DwVeJfDy0z2oL5m_gj6ACfNoDr9EwR1_m8u--3yerolk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1711535298</pqid></control><display><type>article</type><title>Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations</title><source>MEDLINE</source><source>American Chemical Society Publications</source><creator>Karki, Ichhuk ; Wang, Hong ; Geise, Natalie R ; Wilson, Brendan W ; Lewis, James P ; Gullion, Terry</creator><creatorcontrib>Karki, Ichhuk ; Wang, Hong ; Geise, Natalie R ; Wilson, Brendan W ; Lewis, James P ; Gullion, Terry</creatorcontrib><description>The reverse-sequence peptides CysAlaAla and AlaAlaCys may attach to gold nanoparticles through the thiol group, and they differ primarily by whether the charged amino or the carboxylate group is proximal to the sulfur. Alanine residues in these peptides are not expected to interact significantly with the gold surface and serve to place a large separation between the amino and carboxylate groups. Solid-state NMR experiments and DFT calculations were performed to explore the structural differences between CysAlaAla on gold nanoparticles and AlaAlaCys on gold nanoparticles. It is found that the relative positions between the thiol, amino, and carboxylate groups strongly influences the structures of the peptide–gold systems. CysAlaAla orients parallel to the gold surface in a monolayer fashion, whereas AlaAlaCys forms an interdigitating bilayer-like structure that is oriented upright relative to the gold surface.</description><identifier>ISSN: 1520-6106</identifier><identifier>EISSN: 1520-5207</identifier><identifier>DOI: 10.1021/acs.jpcb.5b04299</identifier><identifier>PMID: 26308986</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Carboxylates ; Gold ; Gold - chemistry ; Magnetic Resonance Spectroscopy ; Mathematical analysis ; Metal Nanoparticles - chemistry ; Models, Molecular ; Nanoparticles ; Nuclear magnetic resonance ; Oligopeptides - chemistry ; Peptides ; Protein Conformation ; Quantum Theory ; Residues ; Thiols</subject><ispartof>The journal of physical chemistry. B, 2015-09, Vol.119 (36), p.11998-12006</ispartof><rights>Copyright © 2015 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a369t-73d38e0d2bd994342b100224ebc60ca570df61ac556316ee01e74cb94f20a8af3</citedby><cites>FETCH-LOGICAL-a369t-73d38e0d2bd994342b100224ebc60ca570df61ac556316ee01e74cb94f20a8af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.5b04299$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.jpcb.5b04299$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,2752,27057,27905,27906,56719,56769</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26308986$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Karki, Ichhuk</creatorcontrib><creatorcontrib>Wang, Hong</creatorcontrib><creatorcontrib>Geise, Natalie R</creatorcontrib><creatorcontrib>Wilson, Brendan W</creatorcontrib><creatorcontrib>Lewis, James P</creatorcontrib><creatorcontrib>Gullion, Terry</creatorcontrib><title>Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations</title><title>The journal of physical chemistry. B</title><addtitle>J. Phys. Chem. B</addtitle><description>The reverse-sequence peptides CysAlaAla and AlaAlaCys may attach to gold nanoparticles through the thiol group, and they differ primarily by whether the charged amino or the carboxylate group is proximal to the sulfur. Alanine residues in these peptides are not expected to interact significantly with the gold surface and serve to place a large separation between the amino and carboxylate groups. Solid-state NMR experiments and DFT calculations were performed to explore the structural differences between CysAlaAla on gold nanoparticles and AlaAlaCys on gold nanoparticles. It is found that the relative positions between the thiol, amino, and carboxylate groups strongly influences the structures of the peptide–gold systems. CysAlaAla orients parallel to the gold surface in a monolayer fashion, whereas AlaAlaCys forms an interdigitating bilayer-like structure that is oriented upright relative to the gold surface.</description><subject>Carboxylates</subject><subject>Gold</subject><subject>Gold - chemistry</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Mathematical analysis</subject><subject>Metal Nanoparticles - chemistry</subject><subject>Models, Molecular</subject><subject>Nanoparticles</subject><subject>Nuclear magnetic resonance</subject><subject>Oligopeptides - chemistry</subject><subject>Peptides</subject><subject>Protein Conformation</subject><subject>Quantum Theory</subject><subject>Residues</subject><subject>Thiols</subject><issn>1520-6106</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1DAUha2qiJbCvivkZRdk8E_iJN1VM7RFKkXqDOvIPzeSK48dbKejPgTvjNsZ2CGxsGzJ3zmy74fQOSULShj9LHVaPE5aLRpFatb3R-iUNoxUZbXHh7OgRJygdyk9EsIa1om36IQJTrq-E6fo1ybaCaZsDSQcPL4JzuB76cMkY7baQbrE6xxnnecoHV7ZcYQIXhdaQd4BeLzZBfwATxAT4DX8nPe3MuEVZIhb68Fg9YzXwVlTrbPMgO-_PWDpDV5db_BSOj07mW3w6T16M0qX4MNhP0M_rr9slrfV3febr8uru0py0eeq5YZ3QAxTpu9rXjNFy99YDUoLomXTEjMKKnXTCE4FAKHQ1lr19ciI7OTIz9DFvneKoTw45WFrkwbnpIcwp4G2LeFlwHX7HyilDW9Y3xWU7FEdQ0oRxmGKdivj80DJ8OJrKL6GF1_DwVeJfDy0z2oL5m_gj6ACfNoDr9EwR1_m8u--3yerolk</recordid><startdate>20150910</startdate><enddate>20150910</enddate><creator>Karki, Ichhuk</creator><creator>Wang, Hong</creator><creator>Geise, Natalie R</creator><creator>Wilson, Brendan W</creator><creator>Lewis, James P</creator><creator>Gullion, Terry</creator><general>American Chemical Society</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>7X8</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20150910</creationdate><title>Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations</title><author>Karki, Ichhuk ; Wang, Hong ; Geise, Natalie R ; Wilson, Brendan W ; Lewis, James P ; Gullion, Terry</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a369t-73d38e0d2bd994342b100224ebc60ca570df61ac556316ee01e74cb94f20a8af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Carboxylates</topic><topic>Gold</topic><topic>Gold - chemistry</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Mathematical analysis</topic><topic>Metal Nanoparticles - chemistry</topic><topic>Models, Molecular</topic><topic>Nanoparticles</topic><topic>Nuclear magnetic resonance</topic><topic>Oligopeptides - chemistry</topic><topic>Peptides</topic><topic>Protein Conformation</topic><topic>Quantum Theory</topic><topic>Residues</topic><topic>Thiols</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Karki, Ichhuk</creatorcontrib><creatorcontrib>Wang, Hong</creatorcontrib><creatorcontrib>Geise, Natalie R</creatorcontrib><creatorcontrib>Wilson, Brendan W</creatorcontrib><creatorcontrib>Lewis, James P</creatorcontrib><creatorcontrib>Gullion, Terry</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>The journal of physical chemistry. B</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Karki, Ichhuk</au><au>Wang, Hong</au><au>Geise, Natalie R</au><au>Wilson, Brendan W</au><au>Lewis, James P</au><au>Gullion, Terry</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations</atitle><jtitle>The journal of physical chemistry. B</jtitle><addtitle>J. Phys. Chem. B</addtitle><date>2015-09-10</date><risdate>2015</risdate><volume>119</volume><issue>36</issue><spage>11998</spage><epage>12006</epage><pages>11998-12006</pages><issn>1520-6106</issn><eissn>1520-5207</eissn><abstract>The reverse-sequence peptides CysAlaAla and AlaAlaCys may attach to gold nanoparticles through the thiol group, and they differ primarily by whether the charged amino or the carboxylate group is proximal to the sulfur. Alanine residues in these peptides are not expected to interact significantly with the gold surface and serve to place a large separation between the amino and carboxylate groups. Solid-state NMR experiments and DFT calculations were performed to explore the structural differences between CysAlaAla on gold nanoparticles and AlaAlaCys on gold nanoparticles. It is found that the relative positions between the thiol, amino, and carboxylate groups strongly influences the structures of the peptide–gold systems. CysAlaAla orients parallel to the gold surface in a monolayer fashion, whereas AlaAlaCys forms an interdigitating bilayer-like structure that is oriented upright relative to the gold surface.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>26308986</pmid><doi>10.1021/acs.jpcb.5b04299</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1520-6106 |
| ispartof | The journal of physical chemistry. B, 2015-09, Vol.119 (36), p.11998-12006 |
| issn | 1520-6106 1520-5207 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1770302147 |
| source | MEDLINE; American Chemical Society Publications |
| subjects | Carboxylates Gold Gold - chemistry Magnetic Resonance Spectroscopy Mathematical analysis Metal Nanoparticles - chemistry Models, Molecular Nanoparticles Nuclear magnetic resonance Oligopeptides - chemistry Peptides Protein Conformation Quantum Theory Residues Thiols |
| title | Tripeptides on Gold Nanoparticles: Structural Differences between Two Reverse Sequences as Determined by Solid-State NMR and DFT Calculations |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T15%3A16%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Tripeptides%20on%20Gold%20Nanoparticles:%20Structural%20Differences%20between%20Two%20Reverse%20Sequences%20as%20Determined%20by%20Solid-State%20NMR%20and%20DFT%20Calculations&rft.jtitle=The%20journal%20of%20physical%20chemistry.%20B&rft.au=Karki,%20Ichhuk&rft.date=2015-09-10&rft.volume=119&rft.issue=36&rft.spage=11998&rft.epage=12006&rft.pages=11998-12006&rft.issn=1520-6106&rft.eissn=1520-5207&rft_id=info:doi/10.1021/acs.jpcb.5b04299&rft_dat=%3Cproquest_cross%3E1711535298%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1711535298&rft_id=info:pmid/26308986&rfr_iscdi=true |