Altered Peptide Self‐Assembly and Co‐Assembly with DNA by Modification of Aromatic Residues
Aromatic residues are widely used as building blocks for driving self‐assemblies in natural and designer biomaterials. The noncovalent interactions involving aromatic rings determine proteins’ structure and biofunction. Here, we studied the effects of changes in the proximity of the aromatic rings i...
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| Veröffentlicht in: | ChemMedChem 2021-12, Vol.16 (23), p.3559-3564 |
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| creator | Feng, Ruilu Ni, Rong Chau, Ying |
| description | Aromatic residues are widely used as building blocks for driving self‐assemblies in natural and designer biomaterials. The noncovalent interactions involving aromatic rings determine proteins’ structure and biofunction. Here, we studied the effects of changes in the proximity of the aromatic rings in a self‐assembling peptide for modulating interactions involving the aromatic residues. By changing the distance between the aromatic ring and peptide backbone and replacing the side chain with a sulfur atom, we altered the nanostructures and gene transfection efficiency of peptide‐DNA co‐assemblies. This study demonstrates the significance of subtle alterations in aromatic interactions and facilitates deeper understanding of the aromatic‐involving interactions.
By changing the distance between the aromatic ring and peptide backbone and replacing the side chain with a sulfur atom, we altered the nanostructures and gene transfection efficiency of peptide‐DNA co‐assemblies. This study demonstrates the significance of subtle alterations in aromatic interactions, opens a new avenue to design self‐assembling peptide material, and facilitates deeper understanding of the aromatic‐involving interactions. |
| doi_str_mv | 10.1002/cmdc.202100440 |
| format | Article |
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By changing the distance between the aromatic ring and peptide backbone and replacing the side chain with a sulfur atom, we altered the nanostructures and gene transfection efficiency of peptide‐DNA co‐assemblies. This study demonstrates the significance of subtle alterations in aromatic interactions, opens a new avenue to design self‐assembling peptide material, and facilitates deeper understanding of the aromatic‐involving interactions.</description><identifier>ISSN: 1860-7179</identifier><identifier>EISSN: 1860-7187</identifier><identifier>DOI: 10.1002/cmdc.202100440</identifier><identifier>PMID: 34528415</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Amino Acid Sequence ; Amino Acids, Aromatic - chemistry ; Aromatic compounds ; aromatic interactions ; Assemblies ; Assembling ; Assembly ; Biomaterials ; Biomedical materials ; Deoxyribonucleic acid ; DNA ; DNA - chemistry ; DNA - metabolism ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Gene Transfer Techniques ; HEK293 Cells ; Humans ; Peptides ; Peptides - chemistry ; Peptides - metabolism ; Protein Binding ; Protein Multimerization ; Protein Structure, Secondary ; Residues ; self-assembly ; Sulfur ; Transfection</subject><ispartof>ChemMedChem, 2021-12, Vol.16 (23), p.3559-3564</ispartof><rights>2021 Wiley‐VCH GmbH</rights><rights>2021 Wiley-VCH GmbH.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4130-2e97b78ffcf0eea4ebbfb4294ac3c9a0b96bd84c0499427b5db9225906cd87a33</citedby><cites>FETCH-LOGICAL-c4130-2e97b78ffcf0eea4ebbfb4294ac3c9a0b96bd84c0499427b5db9225906cd87a33</cites><orcidid>0000-0001-7124-3542 ; 0000-0002-1155-5728 ; 0000-0003-1759-934X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fcmdc.202100440$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcmdc.202100440$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34528415$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Feng, Ruilu</creatorcontrib><creatorcontrib>Ni, Rong</creatorcontrib><creatorcontrib>Chau, Ying</creatorcontrib><title>Altered Peptide Self‐Assembly and Co‐Assembly with DNA by Modification of Aromatic Residues</title><title>ChemMedChem</title><addtitle>ChemMedChem</addtitle><description>Aromatic residues are widely used as building blocks for driving self‐assemblies in natural and designer biomaterials. The noncovalent interactions involving aromatic rings determine proteins’ structure and biofunction. Here, we studied the effects of changes in the proximity of the aromatic rings in a self‐assembling peptide for modulating interactions involving the aromatic residues. By changing the distance between the aromatic ring and peptide backbone and replacing the side chain with a sulfur atom, we altered the nanostructures and gene transfection efficiency of peptide‐DNA co‐assemblies. This study demonstrates the significance of subtle alterations in aromatic interactions and facilitates deeper understanding of the aromatic‐involving interactions.
By changing the distance between the aromatic ring and peptide backbone and replacing the side chain with a sulfur atom, we altered the nanostructures and gene transfection efficiency of peptide‐DNA co‐assemblies. This study demonstrates the significance of subtle alterations in aromatic interactions, opens a new avenue to design self‐assembling peptide material, and facilitates deeper understanding of the aromatic‐involving interactions.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids, Aromatic - chemistry</subject><subject>Aromatic compounds</subject><subject>aromatic interactions</subject><subject>Assemblies</subject><subject>Assembling</subject><subject>Assembly</subject><subject>Biomaterials</subject><subject>Biomedical materials</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Gene Transfer Techniques</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Secondary</subject><subject>Residues</subject><subject>self-assembly</subject><subject>Sulfur</subject><subject>Transfection</subject><issn>1860-7179</issn><issn>1860-7187</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EoqWwZYkssU6xHSexl1F4Si0gHmsrfglXSVPsVFV2fALfyJeQqqWwYzVzR2fulS4ApxiNMULkQtVajQkivaAU7YEhZimKMsyy_d2e8QE4CmG2Rhhmh2AQ04QwipMhEHnVGm80fDSL1mkDn01lvz4-8xBMLasOlnMNi-bvZeXaN3h5n0PZwWmjnXWqbF0zh42FuW_qXij4ZILTSxOOwYEtq2BOtnMEXq-vXorbaPJwc1fkk0hRHKOIGJ7JjFmrLDKmpEZKKynhtFSx4iWSPJWaUYUo55RkMtGSE5JwlCrNsjKOR-B847vwzXuf24pZs_TzPlKQFKUME8ZIT403lPJNCN5YsfCuLn0nMBLrPsW6T7Hrs38429ouZW30Dv8psAf4Bli5ynT_2Ilieln8mn8DdH2DQg</recordid><startdate>20211206</startdate><enddate>20211206</enddate><creator>Feng, Ruilu</creator><creator>Ni, Rong</creator><creator>Chau, Ying</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>7TK</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><orcidid>https://orcid.org/0000-0001-7124-3542</orcidid><orcidid>https://orcid.org/0000-0002-1155-5728</orcidid><orcidid>https://orcid.org/0000-0003-1759-934X</orcidid></search><sort><creationdate>20211206</creationdate><title>Altered Peptide Self‐Assembly and Co‐Assembly with DNA by Modification of Aromatic Residues</title><author>Feng, Ruilu ; Ni, Rong ; Chau, Ying</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4130-2e97b78ffcf0eea4ebbfb4294ac3c9a0b96bd84c0499427b5db9225906cd87a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids, Aromatic - chemistry</topic><topic>Aromatic compounds</topic><topic>aromatic interactions</topic><topic>Assemblies</topic><topic>Assembling</topic><topic>Assembly</topic><topic>Biomaterials</topic><topic>Biomedical materials</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA - chemistry</topic><topic>DNA - metabolism</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Gene Transfer Techniques</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - metabolism</topic><topic>Protein Binding</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Secondary</topic><topic>Residues</topic><topic>self-assembly</topic><topic>Sulfur</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Feng, Ruilu</creatorcontrib><creatorcontrib>Ni, Rong</creatorcontrib><creatorcontrib>Chau, Ying</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>Neurosciences 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><collection>Genetics Abstracts</collection><jtitle>ChemMedChem</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Feng, Ruilu</au><au>Ni, Rong</au><au>Chau, Ying</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Altered Peptide Self‐Assembly and Co‐Assembly with DNA by Modification of Aromatic Residues</atitle><jtitle>ChemMedChem</jtitle><addtitle>ChemMedChem</addtitle><date>2021-12-06</date><risdate>2021</risdate><volume>16</volume><issue>23</issue><spage>3559</spage><epage>3564</epage><pages>3559-3564</pages><issn>1860-7179</issn><eissn>1860-7187</eissn><abstract>Aromatic residues are widely used as building blocks for driving self‐assemblies in natural and designer biomaterials. The noncovalent interactions involving aromatic rings determine proteins’ structure and biofunction. Here, we studied the effects of changes in the proximity of the aromatic rings in a self‐assembling peptide for modulating interactions involving the aromatic residues. By changing the distance between the aromatic ring and peptide backbone and replacing the side chain with a sulfur atom, we altered the nanostructures and gene transfection efficiency of peptide‐DNA co‐assemblies. This study demonstrates the significance of subtle alterations in aromatic interactions and facilitates deeper understanding of the aromatic‐involving interactions.
By changing the distance between the aromatic ring and peptide backbone and replacing the side chain with a sulfur atom, we altered the nanostructures and gene transfection efficiency of peptide‐DNA co‐assemblies. This study demonstrates the significance of subtle alterations in aromatic interactions, opens a new avenue to design self‐assembling peptide material, and facilitates deeper understanding of the aromatic‐involving interactions.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>34528415</pmid><doi>10.1002/cmdc.202100440</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0001-7124-3542</orcidid><orcidid>https://orcid.org/0000-0002-1155-5728</orcidid><orcidid>https://orcid.org/0000-0003-1759-934X</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino Acids, Aromatic - chemistry Aromatic compounds aromatic interactions Assemblies Assembling Assembly Biomaterials Biomedical materials Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Gene Transfer Techniques HEK293 Cells Humans Peptides Peptides - chemistry Peptides - metabolism Protein Binding Protein Multimerization Protein Structure, Secondary Residues self-assembly Sulfur Transfection |
| title | Altered Peptide Self‐Assembly and Co‐Assembly with DNA by Modification of Aromatic Residues |
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