OaAEP1-mediated PNA-protein conjugation enables erasable imaging of membrane proteins

We report the use of a protein ligase to covalently ligate a protein to a peptide nucleic acid (PNA). The rapid ligation demands only an N-terminal GL dipeptide in the target protein and a C-terminal NGL tripeptide in the PNA. We demonstrate the versatility of this approach by attaching a PNA strand...

Full description

Saved in:
Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2022-07, Vol.58 (60), p.8448-8451
Main Authors: Lu, Zhangwei, Liu, Yutong, Deng, Yibing, Jia, Bin, Ding, Xuan, Zheng, Peng, Li, Zhe
Format: Article
Language:English
Subjects:
Cell membranes
Conjugation
Nucleic acids
Proteins
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 8451
container_issue 60
container_start_page 8448
container_title Chemical communications (Cambridge, England)
container_volume 58
creator Lu, Zhangwei
Liu, Yutong
Deng, Yibing
Jia, Bin
Ding, Xuan
Zheng, Peng
Li, Zhe
description We report the use of a protein ligase to covalently ligate a protein to a peptide nucleic acid (PNA). The rapid ligation demands only an N-terminal GL dipeptide in the target protein and a C-terminal NGL tripeptide in the PNA. We demonstrate the versatility of this approach by attaching a PNA strand to three different proteins. Lastly, we show that erasable imaging of EGFR on HEK293 cell membranes is achieved with DNA origami nanostructures and toehold-mediated strand displacement.
doi_str_mv 10.1039/d2cc02153f
format article
fullrecord <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_2687723213</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2694601338</sourcerecordid><originalsourceid>FETCH-LOGICAL-p252t-fad651a8188c396ec10629c2652b5c40f8bb6e3b3b3850d8ea88b7c1af1ffed53</originalsourceid><addsrcrecordid>eNpdjj9PwzAQxS0EEqWw8AkssbAY_Cd2nDGqSkGqaAcqsVW2c44SJU6Jk--PKzpxN9wbfu_dQ-iR0RdGRfFacecoZ1L4K7RgQmVEZvr7-qxlQXKRyVt0F2NL0zCpF-iwM-V6z0gPVWMmqPD-sySncZigCdgNoZ1rMzVDwBCM7SBiGE08K9z0pm5CjQePe-jtaALgizHeoxtvuggPl7tEh7f11-qdbHebj1W5JScu-US8qZRkRjOtnSgUOEYVLxxXklvpMuq1tQqETaslrTQYrW3umPHMe6ikWKLnv9z0-GeGOB37JjroulRmmOORK53nXHAmEvr0D22HeQypXaKKTNHEaPELvlhgZA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2694601338</pqid></control><display><type>article</type><title>OaAEP1-mediated PNA-protein conjugation enables erasable imaging of membrane proteins</title><source>Royal Society of Chemistry</source><creator>Lu, Zhangwei ; Liu, Yutong ; Deng, Yibing ; Jia, Bin ; Ding, Xuan ; Zheng, Peng ; Li, Zhe</creator><creatorcontrib>Lu, Zhangwei ; Liu, Yutong ; Deng, Yibing ; Jia, Bin ; Ding, Xuan ; Zheng, Peng ; Li, Zhe</creatorcontrib><description>We report the use of a protein ligase to covalently ligate a protein to a peptide nucleic acid (PNA). The rapid ligation demands only an N-terminal GL dipeptide in the target protein and a C-terminal NGL tripeptide in the PNA. We demonstrate the versatility of this approach by attaching a PNA strand to three different proteins. Lastly, we show that erasable imaging of EGFR on HEK293 cell membranes is achieved with DNA origami nanostructures and toehold-mediated strand displacement.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/d2cc02153f</identifier><language>eng</language><publisher>Cambridge: Royal Society of Chemistry</publisher><subject>Cell membranes ; Conjugation ; Nucleic acids ; Proteins</subject><ispartof>Chemical communications (Cambridge, England), 2022-07, Vol.58 (60), p.8448-8451</ispartof><rights>Copyright Royal Society of Chemistry 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids></links><search><creatorcontrib>Lu, Zhangwei</creatorcontrib><creatorcontrib>Liu, Yutong</creatorcontrib><creatorcontrib>Deng, Yibing</creatorcontrib><creatorcontrib>Jia, Bin</creatorcontrib><creatorcontrib>Ding, Xuan</creatorcontrib><creatorcontrib>Zheng, Peng</creatorcontrib><creatorcontrib>Li, Zhe</creatorcontrib><title>OaAEP1-mediated PNA-protein conjugation enables erasable imaging of membrane proteins</title><title>Chemical communications (Cambridge, England)</title><description>We report the use of a protein ligase to covalently ligate a protein to a peptide nucleic acid (PNA). The rapid ligation demands only an N-terminal GL dipeptide in the target protein and a C-terminal NGL tripeptide in the PNA. We demonstrate the versatility of this approach by attaching a PNA strand to three different proteins. Lastly, we show that erasable imaging of EGFR on HEK293 cell membranes is achieved with DNA origami nanostructures and toehold-mediated strand displacement.</description><subject>Cell membranes</subject><subject>Conjugation</subject><subject>Nucleic acids</subject><subject>Proteins</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNpdjj9PwzAQxS0EEqWw8AkssbAY_Cd2nDGqSkGqaAcqsVW2c44SJU6Jk--PKzpxN9wbfu_dQ-iR0RdGRfFacecoZ1L4K7RgQmVEZvr7-qxlQXKRyVt0F2NL0zCpF-iwM-V6z0gPVWMmqPD-sySncZigCdgNoZ1rMzVDwBCM7SBiGE08K9z0pm5CjQePe-jtaALgizHeoxtvuggPl7tEh7f11-qdbHebj1W5JScu-US8qZRkRjOtnSgUOEYVLxxXklvpMuq1tQqETaslrTQYrW3umPHMe6ikWKLnv9z0-GeGOB37JjroulRmmOORK53nXHAmEvr0D22HeQypXaKKTNHEaPELvlhgZA</recordid><startdate>20220726</startdate><enddate>20220726</enddate><creator>Lu, Zhangwei</creator><creator>Liu, Yutong</creator><creator>Deng, Yibing</creator><creator>Jia, Bin</creator><creator>Ding, Xuan</creator><creator>Zheng, Peng</creator><creator>Li, Zhe</creator><general>Royal Society of Chemistry</general><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>20220726</creationdate><title>OaAEP1-mediated PNA-protein conjugation enables erasable imaging of membrane proteins</title><author>Lu, Zhangwei ; Liu, Yutong ; Deng, Yibing ; Jia, Bin ; Ding, Xuan ; Zheng, Peng ; Li, Zhe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p252t-fad651a8188c396ec10629c2652b5c40f8bb6e3b3b3850d8ea88b7c1af1ffed53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Cell membranes</topic><topic>Conjugation</topic><topic>Nucleic acids</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lu, Zhangwei</creatorcontrib><creatorcontrib>Liu, Yutong</creatorcontrib><creatorcontrib>Deng, Yibing</creatorcontrib><creatorcontrib>Jia, Bin</creatorcontrib><creatorcontrib>Ding, Xuan</creatorcontrib><creatorcontrib>Zheng, Peng</creatorcontrib><creatorcontrib>Li, Zhe</creatorcontrib><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lu, Zhangwei</au><au>Liu, Yutong</au><au>Deng, Yibing</au><au>Jia, Bin</au><au>Ding, Xuan</au><au>Zheng, Peng</au><au>Li, Zhe</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>OaAEP1-mediated PNA-protein conjugation enables erasable imaging of membrane proteins</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><date>2022-07-26</date><risdate>2022</risdate><volume>58</volume><issue>60</issue><spage>8448</spage><epage>8451</epage><pages>8448-8451</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>We report the use of a protein ligase to covalently ligate a protein to a peptide nucleic acid (PNA). The rapid ligation demands only an N-terminal GL dipeptide in the target protein and a C-terminal NGL tripeptide in the PNA. We demonstrate the versatility of this approach by attaching a PNA strand to three different proteins. Lastly, we show that erasable imaging of EGFR on HEK293 cell membranes is achieved with DNA origami nanostructures and toehold-mediated strand displacement.</abstract><cop>Cambridge</cop><pub>Royal Society of Chemistry</pub><doi>10.1039/d2cc02153f</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1359-7345
ispartof Chemical communications (Cambridge, England), 2022-07, Vol.58 (60), p.8448-8451
issn 1359-7345
1364-548X
language eng
recordid cdi_proquest_miscellaneous_2687723213
source Royal Society of Chemistry
subjects Cell membranes
Conjugation
Nucleic acids
Proteins
title OaAEP1-mediated PNA-protein conjugation enables erasable imaging of membrane proteins
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T17%3A04%3A13IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=OaAEP1-mediated%20PNA-protein%20conjugation%20enables%20erasable%20imaging%20of%20membrane%20proteins&rft.jtitle=Chemical%20communications%20(Cambridge,%20England)&rft.au=Lu,%20Zhangwei&rft.date=2022-07-26&rft.volume=58&rft.issue=60&rft.spage=8448&rft.epage=8451&rft.pages=8448-8451&rft.issn=1359-7345&rft.eissn=1364-548X&rft_id=info:doi/10.1039/d2cc02153f&rft_dat=%3Cproquest%3E2694601338%3C/proquest%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-p252t-fad651a8188c396ec10629c2652b5c40f8bb6e3b3b3850d8ea88b7c1af1ffed53%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2694601338&rft_id=info:pmid/&rfr_iscdi=true