Design of a Novel Peptide with Esterolytic Activity toward PET by Mimicking the Catalytic Motif of Serine Hydrolases
Serine hydrolases have become increasingly important for recycling PET plastics. However, their properties are inherently constrained by their 3D structure, which in turn limits the conditions for their application. Considering peptides as catalysts for industrial depolymerization processes can help...
Gespeichert in:
Veröffentlicht in: | The journal of physical chemistry. B 2024-10, Vol.128 (42), p.10363-10372 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 10372 |
---|---|
container_issue | 42 |
container_start_page | 10363 |
container_title | The journal of physical chemistry. B |
container_volume | 128 |
creator | Koch, Jacob Hess, Yan Bak, Christine R. Petersen, Evamaria I. Fojan, Peter |
description | Serine hydrolases have become increasingly important for recycling PET plastics. However, their properties are inherently constrained by their 3D structure, which in turn limits the conditions for their application. Considering peptides as catalysts for industrial depolymerization processes can help us to escape some of these limitations. In this article, a 25 amino acid thermostable peptide, HSH-25, was designed to depolymerize PET. The peptide incorporates a His–Ser–His motif, inspired by the catalytic triad found in the serine hydrolase family, into a β-hairpin fold. Stability of the fold was investigated by molecular dynamics simulations. Esterolytic activity of the peptide toward model substrates was detected within a pH range from pH 7 to pH 9.5. Degradation of polymeric PET substrates was confirmed by atomic force microscopy imaging on spin-coated PET thin films. |
doi_str_mv | 10.1021/acs.jpcb.4c03845 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_3115097903</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3154173134</sourcerecordid><originalsourceid>FETCH-LOGICAL-a252t-67ec1d236090a780f89b5cf47d07683d67654f38a464927bf9f59976f4c9d2193</originalsourceid><addsrcrecordid>eNqNkTtPwzAURi0EolDYmZBHBlrs-BWPVSkPqTwkyhw5jg0uaVxsF5R_T0oLGxKDdT2c7-jqfgCcYDTEKMMXSsfhfKnLIdWI5JTtgAPMMjTontjd_jlGvAcOY5wjlLEs5_ugRyTJGZXkAKRLE91LA72FCt77D1PDR7NMrjLw06VXOInJBF-3yWk40sl9uNTC5D9VqODjZAbLFt65hdNvrnmB6dXAsUpqg9_55Oxa_GSCawy8aavOpKKJR2DPqjqa4-3sg-eryWx8M5g-XN-OR9OB6hZNAy6MxlVGOJJIiRzZXJZMWyoqJHhOKi44o5bkinIqM1FaaZmUgluqZZVhSfrgbONdBv--MjEVCxe1qWvVGL-KBcGMYkEwof9AMUNSSEQ6FG1QHXyMwdhiGdxChbbAqFjXUnS1FOtaim0tXeR0a1-VC1P9Bn566IDzDfAd9avQdHf52_cFCd2YDA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3115097903</pqid></control><display><type>article</type><title>Design of a Novel Peptide with Esterolytic Activity toward PET by Mimicking the Catalytic Motif of Serine Hydrolases</title><source>MEDLINE</source><source>ACS Publications</source><creator>Koch, Jacob ; Hess, Yan ; Bak, Christine R. ; Petersen, Evamaria I. ; Fojan, Peter</creator><creatorcontrib>Koch, Jacob ; Hess, Yan ; Bak, Christine R. ; Petersen, Evamaria I. ; Fojan, Peter</creatorcontrib><description>Serine hydrolases have become increasingly important for recycling PET plastics. However, their properties are inherently constrained by their 3D structure, which in turn limits the conditions for their application. Considering peptides as catalysts for industrial depolymerization processes can help us to escape some of these limitations. In this article, a 25 amino acid thermostable peptide, HSH-25, was designed to depolymerize PET. The peptide incorporates a His–Ser–His motif, inspired by the catalytic triad found in the serine hydrolase family, into a β-hairpin fold. Stability of the fold was investigated by molecular dynamics simulations. Esterolytic activity of the peptide toward model substrates was detected within a pH range from pH 7 to pH 9.5. Degradation of polymeric PET substrates was confirmed by atomic force microscopy imaging on spin-coated PET thin films.</description><identifier>ISSN: 1520-6106</identifier><identifier>ISSN: 1520-5207</identifier><identifier>EISSN: 1520-5207</identifier><identifier>DOI: 10.1021/acs.jpcb.4c03845</identifier><identifier>PMID: 39385493</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Motifs ; atomic force microscopy ; B: Biophysical and Biochemical Systems and Processes ; Catalytic Domain ; depolymerization ; Esters - chemistry ; Esters - metabolism ; family ; Hydrogen-Ion Concentration ; hydrolases ; Hydrolases - chemistry ; Hydrolases - metabolism ; molecular dynamics ; Molecular Dynamics Simulation ; peptides ; Peptides - chemistry ; Peptides - metabolism ; polymers ; serine ; thermal stability</subject><ispartof>The journal of physical chemistry. B, 2024-10, Vol.128 (42), p.10363-10372</ispartof><rights>2024 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-a252t-67ec1d236090a780f89b5cf47d07683d67654f38a464927bf9f59976f4c9d2193</cites><orcidid>0000-0002-0626-4766</orcidid></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.4c03845$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.jpcb.4c03845$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2751,27055,27903,27904,56716,56766</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39385493$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Koch, Jacob</creatorcontrib><creatorcontrib>Hess, Yan</creatorcontrib><creatorcontrib>Bak, Christine R.</creatorcontrib><creatorcontrib>Petersen, Evamaria I.</creatorcontrib><creatorcontrib>Fojan, Peter</creatorcontrib><title>Design of a Novel Peptide with Esterolytic Activity toward PET by Mimicking the Catalytic Motif of Serine Hydrolases</title><title>The journal of physical chemistry. B</title><addtitle>J. Phys. Chem. B</addtitle><description>Serine hydrolases have become increasingly important for recycling PET plastics. However, their properties are inherently constrained by their 3D structure, which in turn limits the conditions for their application. Considering peptides as catalysts for industrial depolymerization processes can help us to escape some of these limitations. In this article, a 25 amino acid thermostable peptide, HSH-25, was designed to depolymerize PET. The peptide incorporates a His–Ser–His motif, inspired by the catalytic triad found in the serine hydrolase family, into a β-hairpin fold. Stability of the fold was investigated by molecular dynamics simulations. Esterolytic activity of the peptide toward model substrates was detected within a pH range from pH 7 to pH 9.5. Degradation of polymeric PET substrates was confirmed by atomic force microscopy imaging on spin-coated PET thin films.</description><subject>Amino Acid Motifs</subject><subject>atomic force microscopy</subject><subject>B: Biophysical and Biochemical Systems and Processes</subject><subject>Catalytic Domain</subject><subject>depolymerization</subject><subject>Esters - chemistry</subject><subject>Esters - metabolism</subject><subject>family</subject><subject>Hydrogen-Ion Concentration</subject><subject>hydrolases</subject><subject>Hydrolases - chemistry</subject><subject>Hydrolases - metabolism</subject><subject>molecular dynamics</subject><subject>Molecular Dynamics Simulation</subject><subject>peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>polymers</subject><subject>serine</subject><subject>thermal stability</subject><issn>1520-6106</issn><issn>1520-5207</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkTtPwzAURi0EolDYmZBHBlrs-BWPVSkPqTwkyhw5jg0uaVxsF5R_T0oLGxKDdT2c7-jqfgCcYDTEKMMXSsfhfKnLIdWI5JTtgAPMMjTontjd_jlGvAcOY5wjlLEs5_ugRyTJGZXkAKRLE91LA72FCt77D1PDR7NMrjLw06VXOInJBF-3yWk40sl9uNTC5D9VqODjZAbLFt65hdNvrnmB6dXAsUpqg9_55Oxa_GSCawy8aavOpKKJR2DPqjqa4-3sg-eryWx8M5g-XN-OR9OB6hZNAy6MxlVGOJJIiRzZXJZMWyoqJHhOKi44o5bkinIqM1FaaZmUgluqZZVhSfrgbONdBv--MjEVCxe1qWvVGL-KBcGMYkEwof9AMUNSSEQ6FG1QHXyMwdhiGdxChbbAqFjXUnS1FOtaim0tXeR0a1-VC1P9Bn566IDzDfAd9avQdHf52_cFCd2YDA</recordid><startdate>20241024</startdate><enddate>20241024</enddate><creator>Koch, Jacob</creator><creator>Hess, Yan</creator><creator>Bak, Christine R.</creator><creator>Petersen, Evamaria I.</creator><creator>Fojan, Peter</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>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0002-0626-4766</orcidid></search><sort><creationdate>20241024</creationdate><title>Design of a Novel Peptide with Esterolytic Activity toward PET by Mimicking the Catalytic Motif of Serine Hydrolases</title><author>Koch, Jacob ; Hess, Yan ; Bak, Christine R. ; Petersen, Evamaria I. ; Fojan, Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a252t-67ec1d236090a780f89b5cf47d07683d67654f38a464927bf9f59976f4c9d2193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Amino Acid Motifs</topic><topic>atomic force microscopy</topic><topic>B: Biophysical and Biochemical Systems and Processes</topic><topic>Catalytic Domain</topic><topic>depolymerization</topic><topic>Esters - chemistry</topic><topic>Esters - metabolism</topic><topic>family</topic><topic>Hydrogen-Ion Concentration</topic><topic>hydrolases</topic><topic>Hydrolases - chemistry</topic><topic>Hydrolases - metabolism</topic><topic>molecular dynamics</topic><topic>Molecular Dynamics Simulation</topic><topic>peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - metabolism</topic><topic>polymers</topic><topic>serine</topic><topic>thermal stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koch, Jacob</creatorcontrib><creatorcontrib>Hess, Yan</creatorcontrib><creatorcontrib>Bak, Christine R.</creatorcontrib><creatorcontrib>Petersen, Evamaria I.</creatorcontrib><creatorcontrib>Fojan, Peter</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>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>The journal of physical chemistry. B</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koch, Jacob</au><au>Hess, Yan</au><au>Bak, Christine R.</au><au>Petersen, Evamaria I.</au><au>Fojan, Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Design of a Novel Peptide with Esterolytic Activity toward PET by Mimicking the Catalytic Motif of Serine Hydrolases</atitle><jtitle>The journal of physical chemistry. B</jtitle><addtitle>J. Phys. Chem. B</addtitle><date>2024-10-24</date><risdate>2024</risdate><volume>128</volume><issue>42</issue><spage>10363</spage><epage>10372</epage><pages>10363-10372</pages><issn>1520-6106</issn><issn>1520-5207</issn><eissn>1520-5207</eissn><abstract>Serine hydrolases have become increasingly important for recycling PET plastics. However, their properties are inherently constrained by their 3D structure, which in turn limits the conditions for their application. Considering peptides as catalysts for industrial depolymerization processes can help us to escape some of these limitations. In this article, a 25 amino acid thermostable peptide, HSH-25, was designed to depolymerize PET. The peptide incorporates a His–Ser–His motif, inspired by the catalytic triad found in the serine hydrolase family, into a β-hairpin fold. Stability of the fold was investigated by molecular dynamics simulations. Esterolytic activity of the peptide toward model substrates was detected within a pH range from pH 7 to pH 9.5. Degradation of polymeric PET substrates was confirmed by atomic force microscopy imaging on spin-coated PET thin films.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>39385493</pmid><doi>10.1021/acs.jpcb.4c03845</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-0626-4766</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1520-6106 |
ispartof | The journal of physical chemistry. B, 2024-10, Vol.128 (42), p.10363-10372 |
issn | 1520-6106 1520-5207 1520-5207 |
language | eng |
recordid | cdi_proquest_miscellaneous_3115097903 |
source | MEDLINE; ACS Publications |
subjects | Amino Acid Motifs atomic force microscopy B: Biophysical and Biochemical Systems and Processes Catalytic Domain depolymerization Esters - chemistry Esters - metabolism family Hydrogen-Ion Concentration hydrolases Hydrolases - chemistry Hydrolases - metabolism molecular dynamics Molecular Dynamics Simulation peptides Peptides - chemistry Peptides - metabolism polymers serine thermal stability |
title | Design of a Novel Peptide with Esterolytic Activity toward PET by Mimicking the Catalytic Motif of Serine Hydrolases |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T20%3A41%3A32IST&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=Design%20of%20a%20Novel%20Peptide%20with%20Esterolytic%20Activity%20toward%20PET%20by%20Mimicking%20the%20Catalytic%20Motif%20of%20Serine%20Hydrolases&rft.jtitle=The%20journal%20of%20physical%20chemistry.%20B&rft.au=Koch,%20Jacob&rft.date=2024-10-24&rft.volume=128&rft.issue=42&rft.spage=10363&rft.epage=10372&rft.pages=10363-10372&rft.issn=1520-6106&rft.eissn=1520-5207&rft_id=info:doi/10.1021/acs.jpcb.4c03845&rft_dat=%3Cproquest_cross%3E3154173134%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=3115097903&rft_id=info:pmid/39385493&rfr_iscdi=true |