Same Day Access to Folded Synthetic Proteins

Understanding protein function is a cornerstone of modern biology. Research centers worldwide dedicate significant efforts to prepare individual proteins for study, the isolation and purification of which can take days to months. We developed a workflow that enables same-day access to functional syn...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of the American Chemical Society 2024-10, Vol.146 (42), p.28696-28706
Hauptverfasser: Callahan, Alex J., Rondon, Aurélie, Reja, Rahi M., Salazar, Lia Lozano, Gandhesiri, Satish, Rodriguez, Jacob, Loas, Andrei, Pentelute, Bradley L.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 28706
container_issue 42
container_start_page 28696
container_title Journal of the American Chemical Society
container_volume 146
creator Callahan, Alex J.
Rondon, Aurélie
Reja, Rahi M.
Salazar, Lia Lozano
Gandhesiri, Satish
Rodriguez, Jacob
Loas, Andrei
Pentelute, Bradley L.
description Understanding protein function is a cornerstone of modern biology. Research centers worldwide dedicate significant efforts to prepare individual proteins for study, the isolation and purification of which can take days to months. We developed a workflow that enables same-day access to functional synthetic proteins. Chemical synthesis provides access to crude protein chains in hours, but the removal of the synthetic side products is typically a days-long process. We find that chemical modifications on side products lead to significant and unpredictable changes in the folding behavior. Consistent with these findings, we discovered that approaches based on biophysical properties characteristic of the folded protein target can discriminate against chemically similar species. Confirming our protocol with nine protein targets, we show that appropriate desalting followed by different folding strategies enables isolation of functional single-domain proteins in hours instead of days. Each target was isolated in under 10 h, including some proteins with post-translational modifications, non-natural amino acids, and disulfide bonds. Rapid biological discovery requires on-demand access to proteins, and the folding pipeline described here is uniquely suited to enabling these efforts. The folding process presented here was not assessed on complex proteins, and therefore, it may require further optimization in those cases.
doi_str_mv 10.1021/jacs.4c05121
format Article
fullrecord <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_proquest_miscellaneous_3154170516</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3115770730</sourcerecordid><originalsourceid>FETCH-LOGICAL-a278t-91d23486f40d0c49df8c64811b7c4085019d2e3431a4a141df49426f1e1cc8643</originalsourceid><addsrcrecordid>eNqNkMFPwyAUh4nRuDm9eTY9arIqDyilx2U6Z7JEk-mZMKBZl7bM0prsv5dmc148yDvAI9_7QT6ErgHfAybwsFHa3zONEyBwgoaQEByHMz9FQ4wxiVPB6QBdeL8JLSMCztGAZqHC8BCNl6qy0aPaRROtrfdR66KZK4010XJXt2vbFjp6a1xri9pforNcld5eHfYR-pg9vU_n8eL1-WU6WcSKpKKNMzCEMsFzhg3WLDO50JwJgFWqGRYJhswQSxkFxRQwMDnLGOE5WNBacEZH6G6fu1al3DZFpZqddKqQ88lC9neYibAY_4LA3u7ZbeM-O-tbWRVe27JUtXWdlxQSBmmww_-BQpKmOKU4oOM9qhvnfWPz4zcAy1677LXLg_aA3xySu1VlzRH-8fz7dD-1cV1TB39_Z30DiROGPQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3115770730</pqid></control><display><type>article</type><title>Same Day Access to Folded Synthetic Proteins</title><source>American Chemical Society Journals</source><creator>Callahan, Alex J. ; Rondon, Aurélie ; Reja, Rahi M. ; Salazar, Lia Lozano ; Gandhesiri, Satish ; Rodriguez, Jacob ; Loas, Andrei ; Pentelute, Bradley L.</creator><creatorcontrib>Callahan, Alex J. ; Rondon, Aurélie ; Reja, Rahi M. ; Salazar, Lia Lozano ; Gandhesiri, Satish ; Rodriguez, Jacob ; Loas, Andrei ; Pentelute, Bradley L.</creatorcontrib><description>Understanding protein function is a cornerstone of modern biology. Research centers worldwide dedicate significant efforts to prepare individual proteins for study, the isolation and purification of which can take days to months. We developed a workflow that enables same-day access to functional synthetic proteins. Chemical synthesis provides access to crude protein chains in hours, but the removal of the synthetic side products is typically a days-long process. We find that chemical modifications on side products lead to significant and unpredictable changes in the folding behavior. Consistent with these findings, we discovered that approaches based on biophysical properties characteristic of the folded protein target can discriminate against chemically similar species. Confirming our protocol with nine protein targets, we show that appropriate desalting followed by different folding strategies enables isolation of functional single-domain proteins in hours instead of days. Each target was isolated in under 10 h, including some proteins with post-translational modifications, non-natural amino acids, and disulfide bonds. Rapid biological discovery requires on-demand access to proteins, and the folding pipeline described here is uniquely suited to enabling these efforts. The folding process presented here was not assessed on complex proteins, and therefore, it may require further optimization in those cases.</description><identifier>ISSN: 0002-7863</identifier><identifier>ISSN: 1520-5126</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/jacs.4c05121</identifier><identifier>PMID: 39393021</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Chemical Sciences ; crude protein ; disulfides ; species ; synthesis</subject><ispartof>Journal of the American Chemical Society, 2024-10, Vol.146 (42), p.28696-28706</ispartof><rights>2024 American Chemical Society</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-a278t-91d23486f40d0c49df8c64811b7c4085019d2e3431a4a141df49426f1e1cc8643</cites><orcidid>0000-0003-1202-5013 ; 0000-0001-9981-2460 ; 0000-0001-5640-1645 ; 0000-0002-7242-801X</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/jacs.4c05121$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jacs.4c05121$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,776,780,881,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39393021$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-04888846$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Callahan, Alex J.</creatorcontrib><creatorcontrib>Rondon, Aurélie</creatorcontrib><creatorcontrib>Reja, Rahi M.</creatorcontrib><creatorcontrib>Salazar, Lia Lozano</creatorcontrib><creatorcontrib>Gandhesiri, Satish</creatorcontrib><creatorcontrib>Rodriguez, Jacob</creatorcontrib><creatorcontrib>Loas, Andrei</creatorcontrib><creatorcontrib>Pentelute, Bradley L.</creatorcontrib><title>Same Day Access to Folded Synthetic Proteins</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>Understanding protein function is a cornerstone of modern biology. Research centers worldwide dedicate significant efforts to prepare individual proteins for study, the isolation and purification of which can take days to months. We developed a workflow that enables same-day access to functional synthetic proteins. Chemical synthesis provides access to crude protein chains in hours, but the removal of the synthetic side products is typically a days-long process. We find that chemical modifications on side products lead to significant and unpredictable changes in the folding behavior. Consistent with these findings, we discovered that approaches based on biophysical properties characteristic of the folded protein target can discriminate against chemically similar species. Confirming our protocol with nine protein targets, we show that appropriate desalting followed by different folding strategies enables isolation of functional single-domain proteins in hours instead of days. Each target was isolated in under 10 h, including some proteins with post-translational modifications, non-natural amino acids, and disulfide bonds. Rapid biological discovery requires on-demand access to proteins, and the folding pipeline described here is uniquely suited to enabling these efforts. The folding process presented here was not assessed on complex proteins, and therefore, it may require further optimization in those cases.</description><subject>Chemical Sciences</subject><subject>crude protein</subject><subject>disulfides</subject><subject>species</subject><subject>synthesis</subject><issn>0002-7863</issn><issn>1520-5126</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNqNkMFPwyAUh4nRuDm9eTY9arIqDyilx2U6Z7JEk-mZMKBZl7bM0prsv5dmc148yDvAI9_7QT6ErgHfAybwsFHa3zONEyBwgoaQEByHMz9FQ4wxiVPB6QBdeL8JLSMCztGAZqHC8BCNl6qy0aPaRROtrfdR66KZK4010XJXt2vbFjp6a1xri9pforNcld5eHfYR-pg9vU_n8eL1-WU6WcSKpKKNMzCEMsFzhg3WLDO50JwJgFWqGRYJhswQSxkFxRQwMDnLGOE5WNBacEZH6G6fu1al3DZFpZqddKqQ88lC9neYibAY_4LA3u7ZbeM-O-tbWRVe27JUtXWdlxQSBmmww_-BQpKmOKU4oOM9qhvnfWPz4zcAy1677LXLg_aA3xySu1VlzRH-8fz7dD-1cV1TB39_Z30DiROGPQ</recordid><startdate>20241011</startdate><enddate>20241011</enddate><creator>Callahan, Alex J.</creator><creator>Rondon, Aurélie</creator><creator>Reja, Rahi M.</creator><creator>Salazar, Lia Lozano</creator><creator>Gandhesiri, Satish</creator><creator>Rodriguez, Jacob</creator><creator>Loas, Andrei</creator><creator>Pentelute, Bradley L.</creator><general>American Chemical Society</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-1202-5013</orcidid><orcidid>https://orcid.org/0000-0001-9981-2460</orcidid><orcidid>https://orcid.org/0000-0001-5640-1645</orcidid><orcidid>https://orcid.org/0000-0002-7242-801X</orcidid></search><sort><creationdate>20241011</creationdate><title>Same Day Access to Folded Synthetic Proteins</title><author>Callahan, Alex J. ; Rondon, Aurélie ; Reja, Rahi M. ; Salazar, Lia Lozano ; Gandhesiri, Satish ; Rodriguez, Jacob ; Loas, Andrei ; Pentelute, Bradley L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a278t-91d23486f40d0c49df8c64811b7c4085019d2e3431a4a141df49426f1e1cc8643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Chemical Sciences</topic><topic>crude protein</topic><topic>disulfides</topic><topic>species</topic><topic>synthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Callahan, Alex J.</creatorcontrib><creatorcontrib>Rondon, Aurélie</creatorcontrib><creatorcontrib>Reja, Rahi M.</creatorcontrib><creatorcontrib>Salazar, Lia Lozano</creatorcontrib><creatorcontrib>Gandhesiri, Satish</creatorcontrib><creatorcontrib>Rodriguez, Jacob</creatorcontrib><creatorcontrib>Loas, Andrei</creatorcontrib><creatorcontrib>Pentelute, Bradley L.</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Callahan, Alex J.</au><au>Rondon, Aurélie</au><au>Reja, Rahi M.</au><au>Salazar, Lia Lozano</au><au>Gandhesiri, Satish</au><au>Rodriguez, Jacob</au><au>Loas, Andrei</au><au>Pentelute, Bradley L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Same Day Access to Folded Synthetic Proteins</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2024-10-11</date><risdate>2024</risdate><volume>146</volume><issue>42</issue><spage>28696</spage><epage>28706</epage><pages>28696-28706</pages><issn>0002-7863</issn><issn>1520-5126</issn><eissn>1520-5126</eissn><abstract>Understanding protein function is a cornerstone of modern biology. Research centers worldwide dedicate significant efforts to prepare individual proteins for study, the isolation and purification of which can take days to months. We developed a workflow that enables same-day access to functional synthetic proteins. Chemical synthesis provides access to crude protein chains in hours, but the removal of the synthetic side products is typically a days-long process. We find that chemical modifications on side products lead to significant and unpredictable changes in the folding behavior. Consistent with these findings, we discovered that approaches based on biophysical properties characteristic of the folded protein target can discriminate against chemically similar species. Confirming our protocol with nine protein targets, we show that appropriate desalting followed by different folding strategies enables isolation of functional single-domain proteins in hours instead of days. Each target was isolated in under 10 h, including some proteins with post-translational modifications, non-natural amino acids, and disulfide bonds. Rapid biological discovery requires on-demand access to proteins, and the folding pipeline described here is uniquely suited to enabling these efforts. The folding process presented here was not assessed on complex proteins, and therefore, it may require further optimization in those cases.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>39393021</pmid><doi>10.1021/jacs.4c05121</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0003-1202-5013</orcidid><orcidid>https://orcid.org/0000-0001-9981-2460</orcidid><orcidid>https://orcid.org/0000-0001-5640-1645</orcidid><orcidid>https://orcid.org/0000-0002-7242-801X</orcidid></addata></record>
fulltext fulltext
identifier ISSN: 0002-7863
ispartof Journal of the American Chemical Society, 2024-10, Vol.146 (42), p.28696-28706
issn 0002-7863
1520-5126
1520-5126
language eng
recordid cdi_proquest_miscellaneous_3154170516
source American Chemical Society Journals
subjects Chemical Sciences
crude protein
disulfides
species
synthesis
title Same Day Access to Folded Synthetic Proteins
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T20%3A27%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Same%20Day%20Access%20to%20Folded%20Synthetic%20Proteins&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Callahan,%20Alex%20J.&rft.date=2024-10-11&rft.volume=146&rft.issue=42&rft.spage=28696&rft.epage=28706&rft.pages=28696-28706&rft.issn=0002-7863&rft.eissn=1520-5126&rft_id=info:doi/10.1021/jacs.4c05121&rft_dat=%3Cproquest_hal_p%3E3115770730%3C/proquest_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=3115770730&rft_id=info:pmid/39393021&rfr_iscdi=true