Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues
A novel strategy to generate adhesive protein analogues by enzyme‐induced polymerization of peptides is reported. Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa‐moieties with free thiols from cysteine residues, thereby lin...
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| Veröffentlicht in: | Angewandte Chemie International Edition 2018-11, Vol.57 (48), p.15728-15732 |
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| creator | Horsch, Justus Wilke, Patrick Pretzler, Matthias Seuss, Maximilian Melnyk, Inga Remmler, Dario Fery, Andreas Rompel, Annette Börner, Hans G. |
| description | A novel strategy to generate adhesive protein analogues by enzyme‐induced polymerization of peptides is reported. Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa‐moieties with free thiols from cysteine residues, thereby linking unimers and generating adhesive polymers. The resulting artificial protein analogues show strong adsorption to different surfaces, even resisting hypersaline conditions. Remarkable adhesion energies of up to 10.9 mJ m−2 are found in single adhesion events and average values are superior to those reported for mussel foot proteins that constitute the gluing interfaces.
Mussel glue protein mimics: Adhesive mussel‐inspired protein analogues were prepared by an enzyme‐induced polymerization of oligopeptides. The polymers are generated by the formation of cysteinyldopa linkages that contribute to cohesion and adhesion of the protein analogues. Aspects of adhesion properties of mussel foot proteins were mimicked without the need to extract and purify or express native proteins. |
| doi_str_mv | 10.1002/anie.201809587 |
| format | Article |
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Mussel glue protein mimics: Adhesive mussel‐inspired protein analogues were prepared by an enzyme‐induced polymerization of oligopeptides. The polymers are generated by the formation of cysteinyldopa linkages that contribute to cohesion and adhesion of the protein analogues. Aspects of adhesion properties of mussel foot proteins were mimicked without the need to extract and purify or express native proteins.</description><edition>International ed. in English</edition><identifier>ISSN: 1433-7851</identifier><identifier>ISSN: 1521-3773</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.201809587</identifier><identifier>PMID: 30246912</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Adhesion ; Adhesives ; Adhesives - chemistry ; Adhesives - metabolism ; Adsorption ; Animals ; Benzoquinones - chemistry ; Benzoquinones - metabolism ; Biomimetic Materials - chemistry ; Biomimetic Materials - metabolism ; Bivalvia - chemistry ; Bivalvia - metabolism ; Communication ; Communications ; Cysteine - chemistry ; Cysteine - metabolism ; Dihydroxyphenylalanine - analogs & derivatives ; Dihydroxyphenylalanine - chemistry ; Dihydroxyphenylalanine - metabolism ; enzyme-induced polymerization ; Glues ; Gluing ; Interfaces ; Molecular Structure ; Mollusks ; Monophenol Monooxygenase - chemistry ; Monophenol Monooxygenase - metabolism ; mussel glue ; Mussels ; Oxidation ; Peptides ; Polymerization ; Polymers ; Proteins ; Proteins - chemistry ; Proteins - metabolism ; Residues ; Surface Properties ; synthetic protein mimics ; Thiols ; Tyrosinase ; tyrosinase activation ; Tyrosine</subject><ispartof>Angewandte Chemie International Edition, 2018-11, Vol.57 (48), p.15728-15732</ispartof><rights>2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.</rights><rights>2018 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5347-2e11dee6020eafd97c1290e34118a762515119281a93df1323abeb729629db1f3</citedby><cites>FETCH-LOGICAL-c5347-2e11dee6020eafd97c1290e34118a762515119281a93df1323abeb729629db1f3</cites><orcidid>0000-0001-8662-5105 ; 0000-0001-6692-3762 ; 0000-0002-5919-0553 ; 0000-0001-9333-9780 ; 0000-0003-2637-6738</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%2Fanie.201809587$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fanie.201809587$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30246912$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Horsch, Justus</creatorcontrib><creatorcontrib>Wilke, Patrick</creatorcontrib><creatorcontrib>Pretzler, Matthias</creatorcontrib><creatorcontrib>Seuss, Maximilian</creatorcontrib><creatorcontrib>Melnyk, Inga</creatorcontrib><creatorcontrib>Remmler, Dario</creatorcontrib><creatorcontrib>Fery, Andreas</creatorcontrib><creatorcontrib>Rompel, Annette</creatorcontrib><creatorcontrib>Börner, Hans G.</creatorcontrib><title>Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues</title><title>Angewandte Chemie International Edition</title><addtitle>Angew Chem Int Ed Engl</addtitle><description>A novel strategy to generate adhesive protein analogues by enzyme‐induced polymerization of peptides is reported. Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa‐moieties with free thiols from cysteine residues, thereby linking unimers and generating adhesive polymers. The resulting artificial protein analogues show strong adsorption to different surfaces, even resisting hypersaline conditions. Remarkable adhesion energies of up to 10.9 mJ m−2 are found in single adhesion events and average values are superior to those reported for mussel foot proteins that constitute the gluing interfaces.
Mussel glue protein mimics: Adhesive mussel‐inspired protein analogues were prepared by an enzyme‐induced polymerization of oligopeptides. The polymers are generated by the formation of cysteinyldopa linkages that contribute to cohesion and adhesion of the protein analogues. Aspects of adhesion properties of mussel foot proteins were mimicked without the need to extract and purify or express native proteins.</description><subject>Adhesion</subject><subject>Adhesives</subject><subject>Adhesives - chemistry</subject><subject>Adhesives - metabolism</subject><subject>Adsorption</subject><subject>Animals</subject><subject>Benzoquinones - chemistry</subject><subject>Benzoquinones - metabolism</subject><subject>Biomimetic Materials - chemistry</subject><subject>Biomimetic Materials - metabolism</subject><subject>Bivalvia - chemistry</subject><subject>Bivalvia - metabolism</subject><subject>Communication</subject><subject>Communications</subject><subject>Cysteine - chemistry</subject><subject>Cysteine - metabolism</subject><subject>Dihydroxyphenylalanine - analogs & derivatives</subject><subject>Dihydroxyphenylalanine - chemistry</subject><subject>Dihydroxyphenylalanine - metabolism</subject><subject>enzyme-induced polymerization</subject><subject>Glues</subject><subject>Gluing</subject><subject>Interfaces</subject><subject>Molecular Structure</subject><subject>Mollusks</subject><subject>Monophenol Monooxygenase - chemistry</subject><subject>Monophenol Monooxygenase - metabolism</subject><subject>mussel glue</subject><subject>Mussels</subject><subject>Oxidation</subject><subject>Peptides</subject><subject>Polymerization</subject><subject>Polymers</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Residues</subject><subject>Surface Properties</subject><subject>synthetic protein mimics</subject><subject>Thiols</subject><subject>Tyrosinase</subject><subject>tyrosinase activation</subject><subject>Tyrosine</subject><issn>1433-7851</issn><issn>1521-3773</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EoqVw5YgsceGSxWPHsc0BqSptqbTQCoo4Wt5k0rpk7WInrba_Hle7LB-XnmakeebRjF5CXgKbAWP8rQseZ5yBZkZq9YjsguRQCaXE49LXQlRKS9ghz3K-KrzWrHlKdgTjdWOA75LvZ3FYLTH5Ox8u6Nz_QPppyhmHTD_Ed_Q83rrU0a-rMF7i6NvNkB7FONKzFEf0IVMXOvoFs8-jCyM9HibMz8mT3g0ZX2zqHvl2dHh-8LGanx6fHOzPq1aKWlUcATrEhnGGru-MaoEbhqIG0E41XIIEMFyDM6LrQXDhFrhQ3DTcdAvoxR55v_ZeT4sldi2GMbnBXie_dGllo_P230nwl_Yi3tiGa260KII3G0GKP8vho1363OIwuIBxypYDgKo5r2VBX_-HXsUphfJeoYRsQDZMF2q2ptoUc07Yb48BZu8zs_eZ2W1mZeHV3y9s8d8hFcCsgVs_4OoBnd3_fHL4R_4L6uSjOA</recordid><startdate>20181126</startdate><enddate>20181126</enddate><creator>Horsch, Justus</creator><creator>Wilke, Patrick</creator><creator>Pretzler, Matthias</creator><creator>Seuss, Maximilian</creator><creator>Melnyk, Inga</creator><creator>Remmler, Dario</creator><creator>Fery, Andreas</creator><creator>Rompel, Annette</creator><creator>Börner, Hans G.</creator><general>Wiley Subscription Services, Inc</general><general>John Wiley and Sons Inc</general><scope>24P</scope><scope>WIN</scope><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>7TM</scope><scope>K9.</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-8662-5105</orcidid><orcidid>https://orcid.org/0000-0001-6692-3762</orcidid><orcidid>https://orcid.org/0000-0002-5919-0553</orcidid><orcidid>https://orcid.org/0000-0001-9333-9780</orcidid><orcidid>https://orcid.org/0000-0003-2637-6738</orcidid></search><sort><creationdate>20181126</creationdate><title>Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues</title><author>Horsch, Justus ; Wilke, Patrick ; Pretzler, Matthias ; Seuss, Maximilian ; Melnyk, Inga ; Remmler, Dario ; Fery, Andreas ; Rompel, Annette ; Börner, Hans G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5347-2e11dee6020eafd97c1290e34118a762515119281a93df1323abeb729629db1f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Adhesion</topic><topic>Adhesives</topic><topic>Adhesives - chemistry</topic><topic>Adhesives - metabolism</topic><topic>Adsorption</topic><topic>Animals</topic><topic>Benzoquinones - chemistry</topic><topic>Benzoquinones - metabolism</topic><topic>Biomimetic Materials - chemistry</topic><topic>Biomimetic Materials - metabolism</topic><topic>Bivalvia - chemistry</topic><topic>Bivalvia - metabolism</topic><topic>Communication</topic><topic>Communications</topic><topic>Cysteine - chemistry</topic><topic>Cysteine - metabolism</topic><topic>Dihydroxyphenylalanine - analogs & derivatives</topic><topic>Dihydroxyphenylalanine - chemistry</topic><topic>Dihydroxyphenylalanine - metabolism</topic><topic>enzyme-induced polymerization</topic><topic>Glues</topic><topic>Gluing</topic><topic>Interfaces</topic><topic>Molecular Structure</topic><topic>Mollusks</topic><topic>Monophenol Monooxygenase - chemistry</topic><topic>Monophenol Monooxygenase - metabolism</topic><topic>mussel glue</topic><topic>Mussels</topic><topic>Oxidation</topic><topic>Peptides</topic><topic>Polymerization</topic><topic>Polymers</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>Residues</topic><topic>Surface Properties</topic><topic>synthetic protein mimics</topic><topic>Thiols</topic><topic>Tyrosinase</topic><topic>tyrosinase activation</topic><topic>Tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Horsch, Justus</creatorcontrib><creatorcontrib>Wilke, Patrick</creatorcontrib><creatorcontrib>Pretzler, Matthias</creatorcontrib><creatorcontrib>Seuss, Maximilian</creatorcontrib><creatorcontrib>Melnyk, Inga</creatorcontrib><creatorcontrib>Remmler, Dario</creatorcontrib><creatorcontrib>Fery, Andreas</creatorcontrib><creatorcontrib>Rompel, Annette</creatorcontrib><creatorcontrib>Börner, Hans G.</creatorcontrib><collection>Wiley-Blackwell Open Access Titles</collection><collection>Wiley Free Content</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Angewandte Chemie International Edition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Horsch, Justus</au><au>Wilke, Patrick</au><au>Pretzler, Matthias</au><au>Seuss, Maximilian</au><au>Melnyk, Inga</au><au>Remmler, Dario</au><au>Fery, Andreas</au><au>Rompel, Annette</au><au>Börner, Hans G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew Chem Int Ed Engl</addtitle><date>2018-11-26</date><risdate>2018</risdate><volume>57</volume><issue>48</issue><spage>15728</spage><epage>15732</epage><pages>15728-15732</pages><issn>1433-7851</issn><issn>1521-3773</issn><eissn>1521-3773</eissn><abstract>A novel strategy to generate adhesive protein analogues by enzyme‐induced polymerization of peptides is reported. Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa‐moieties with free thiols from cysteine residues, thereby linking unimers and generating adhesive polymers. The resulting artificial protein analogues show strong adsorption to different surfaces, even resisting hypersaline conditions. Remarkable adhesion energies of up to 10.9 mJ m−2 are found in single adhesion events and average values are superior to those reported for mussel foot proteins that constitute the gluing interfaces.
Mussel glue protein mimics: Adhesive mussel‐inspired protein analogues were prepared by an enzyme‐induced polymerization of oligopeptides. The polymers are generated by the formation of cysteinyldopa linkages that contribute to cohesion and adhesion of the protein analogues. Aspects of adhesion properties of mussel foot proteins were mimicked without the need to extract and purify or express native proteins.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>30246912</pmid><doi>10.1002/anie.201809587</doi><tpages>5</tpages><edition>International ed. in English</edition><orcidid>https://orcid.org/0000-0001-8662-5105</orcidid><orcidid>https://orcid.org/0000-0001-6692-3762</orcidid><orcidid>https://orcid.org/0000-0002-5919-0553</orcidid><orcidid>https://orcid.org/0000-0001-9333-9780</orcidid><orcidid>https://orcid.org/0000-0003-2637-6738</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adhesion Adhesives Adhesives - chemistry Adhesives - metabolism Adsorption Animals Benzoquinones - chemistry Benzoquinones - metabolism Biomimetic Materials - chemistry Biomimetic Materials - metabolism Bivalvia - chemistry Bivalvia - metabolism Communication Communications Cysteine - chemistry Cysteine - metabolism Dihydroxyphenylalanine - analogs & derivatives Dihydroxyphenylalanine - chemistry Dihydroxyphenylalanine - metabolism enzyme-induced polymerization Glues Gluing Interfaces Molecular Structure Mollusks Monophenol Monooxygenase - chemistry Monophenol Monooxygenase - metabolism mussel glue Mussels Oxidation Peptides Polymerization Polymers Proteins Proteins - chemistry Proteins - metabolism Residues Surface Properties synthetic protein mimics Thiols Tyrosinase tyrosinase activation Tyrosine |
| title | Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues |
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