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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The journal of physical chemistry. B 2024-10, Vol.128 (42), p.10363-10372
Hauptverfasser: Koch, Jacob, Hess, Yan, Bak, Christine R., Petersen, Evamaria I., Fojan, Peter
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