Loading…
Effect of Preorganized Charge‐Display on the Cell‐Penetrating Properties of Cationic Peptides
The effect of preorganized versus undefined charge display on the cellular uptake of cationic cell‐penetrating peptides (CPPs) was investigated by comparing conformationally well‐defined guanidinylated oligoprolines with flexible oligoarginines. Flow cytometry and confocal microscopy studies with di...
Saved in:
| Published in: | Angewandte Chemie International Edition 2017-01, Vol.56 (1), p.122-126 |
|---|---|
| Main Authors: | , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c5049-d173ebf6a013a5af9f20eb27d10d28fcc114c8ebfae0c2e419fcd2e78aa8adc53 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c5049-d173ebf6a013a5af9f20eb27d10d28fcc114c8ebfae0c2e419fcd2e78aa8adc53 |
| container_end_page | 126 |
| container_issue | 1 |
| container_start_page | 122 |
| container_title | Angewandte Chemie International Edition |
| container_volume | 56 |
| creator | Nagel, Yvonne A. Raschle, Philipp S. Wennemers, Helma |
| description | The effect of preorganized versus undefined charge display on the cellular uptake of cationic cell‐penetrating peptides (CPPs) was investigated by comparing conformationally well‐defined guanidinylated oligoprolines with flexible oligoarginines. Flow cytometry and confocal microscopy studies with different cancer cell lines (HeLa, MCF‐7, and HT‐29) showed that preorganization of cationic charges in lateral distances of ≈9 Å enhanced the cellular uptake of CPPs. Binding affinity measurements revealed tighter binding of analogues of cell‐surface glycans to the guanidinylated octaproline with localized charges compared to flexible octaarginine, a finding that was further correlated to the cellular uptake by studies with CHO cells deficient in glycans on the outer plasma membrane.
Matching charges: Cationic oligoprolines with charges at lateral distances of 9 Å penetrate into cancer cells at submicromolar concentrations. The cellular uptake correlates with binding affinity to the cell‐surface glycan analogue heparin with comparable distances between anionic sulfate moieties. |
| doi_str_mv | 10.1002/anie.201607649 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1845249646</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1845249646</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5049-d173ebf6a013a5af9f20eb27d10d28fcc114c8ebfae0c2e419fcd2e78aa8adc53</originalsourceid><addsrcrecordid>eNqFkU1LAzEQhoMofl89yoIXL1uT7EeyR1mrFor2oOeQZidtynazJluknvwJ_kZ_iSmtFTwoc5hheOZh4EXojOAewZheycZAj2KSY5anxQ46JBklccJYshvmNElixjNygI68nwWec5zvowPKCow5zg6R7GsNqousjkYOrJsE4RtUUTmVbgKf7x83xre1XEa2ibopRCXUddiOoIHOyc40k3BnW3CdAb-ylGFpG6OiEbSdqcCfoD0taw-nm36Mnm_7T-V9PHy8G5TXw1hlOC3iirAExjqXmCQyk7rQFMOYsorginKtFCGp4oGQgBWFlBRaVRQYl5LLSmXJMbpce1tnXxbgOzE3XoV3ZQN24QXhaUbTIk_zgF78Qmd24ZrwnaCY5gUJxf-iCM8SynLKaaB6a0o5670DLVpn5tItBcFiFZFYRSS2EYWD8412MZ5DtcW_MwlAsQZeTQ3Lf3Ti-mHQ_5F_AeKFn3s</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1853276282</pqid></control><display><type>article</type><title>Effect of Preorganized Charge‐Display on the Cell‐Penetrating Properties of Cationic Peptides</title><source>Wiley</source><creator>Nagel, Yvonne A. ; Raschle, Philipp S. ; Wennemers, Helma</creator><creatorcontrib>Nagel, Yvonne A. ; Raschle, Philipp S. ; Wennemers, Helma</creatorcontrib><description>The effect of preorganized versus undefined charge display on the cellular uptake of cationic cell‐penetrating peptides (CPPs) was investigated by comparing conformationally well‐defined guanidinylated oligoprolines with flexible oligoarginines. Flow cytometry and confocal microscopy studies with different cancer cell lines (HeLa, MCF‐7, and HT‐29) showed that preorganization of cationic charges in lateral distances of ≈9 Å enhanced the cellular uptake of CPPs. Binding affinity measurements revealed tighter binding of analogues of cell‐surface glycans to the guanidinylated octaproline with localized charges compared to flexible octaarginine, a finding that was further correlated to the cellular uptake by studies with CHO cells deficient in glycans on the outer plasma membrane.
Matching charges: Cationic oligoprolines with charges at lateral distances of 9 Å penetrate into cancer cells at submicromolar concentrations. The cellular uptake correlates with binding affinity to the cell‐surface glycan analogue heparin with comparable distances between anionic sulfate moieties.</description><edition>International ed. in English</edition><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.201607649</identifier><identifier>PMID: 27900805</identifier><identifier>CODEN: ACIEAY</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Animals ; Anticoagulants ; arginine ; Binding ; Cancer ; Cationic peptides ; Cations ; Cations - chemistry ; Cations - pharmacokinetics ; Cell Membrane Permeability ; Cell surface ; Cell-Penetrating Peptides - chemistry ; Cell-Penetrating Peptides - pharmacokinetics ; cellular uptake ; CHO Cells ; Confocal microscopy ; Cricetulus ; Cytometry ; Flow cytometry ; HeLa Cells ; heparin ; HT29 Cells ; Humans ; MCF-7 Cells ; Microscopy ; Oligopeptides - chemistry ; Oligopeptides - pharmacokinetics ; oligoproline ; Peptides ; Polysaccharides ; Proline - analogs & derivatives ; Proline - pharmacokinetics ; Static Electricity ; Tumor cell lines</subject><ispartof>Angewandte Chemie International Edition, 2017-01, Vol.56 (1), p.122-126</ispartof><rights>2017 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5049-d173ebf6a013a5af9f20eb27d10d28fcc114c8ebfae0c2e419fcd2e78aa8adc53</citedby><cites>FETCH-LOGICAL-c5049-d173ebf6a013a5af9f20eb27d10d28fcc114c8ebfae0c2e419fcd2e78aa8adc53</cites><orcidid>0000-0002-3075-5741</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27900805$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nagel, Yvonne A.</creatorcontrib><creatorcontrib>Raschle, Philipp S.</creatorcontrib><creatorcontrib>Wennemers, Helma</creatorcontrib><title>Effect of Preorganized Charge‐Display on the Cell‐Penetrating Properties of Cationic Peptides</title><title>Angewandte Chemie International Edition</title><addtitle>Angew Chem Int Ed Engl</addtitle><description>The effect of preorganized versus undefined charge display on the cellular uptake of cationic cell‐penetrating peptides (CPPs) was investigated by comparing conformationally well‐defined guanidinylated oligoprolines with flexible oligoarginines. Flow cytometry and confocal microscopy studies with different cancer cell lines (HeLa, MCF‐7, and HT‐29) showed that preorganization of cationic charges in lateral distances of ≈9 Å enhanced the cellular uptake of CPPs. Binding affinity measurements revealed tighter binding of analogues of cell‐surface glycans to the guanidinylated octaproline with localized charges compared to flexible octaarginine, a finding that was further correlated to the cellular uptake by studies with CHO cells deficient in glycans on the outer plasma membrane.
Matching charges: Cationic oligoprolines with charges at lateral distances of 9 Å penetrate into cancer cells at submicromolar concentrations. The cellular uptake correlates with binding affinity to the cell‐surface glycan analogue heparin with comparable distances between anionic sulfate moieties.</description><subject>Animals</subject><subject>Anticoagulants</subject><subject>arginine</subject><subject>Binding</subject><subject>Cancer</subject><subject>Cationic peptides</subject><subject>Cations</subject><subject>Cations - chemistry</subject><subject>Cations - pharmacokinetics</subject><subject>Cell Membrane Permeability</subject><subject>Cell surface</subject><subject>Cell-Penetrating Peptides - chemistry</subject><subject>Cell-Penetrating Peptides - pharmacokinetics</subject><subject>cellular uptake</subject><subject>CHO Cells</subject><subject>Confocal microscopy</subject><subject>Cricetulus</subject><subject>Cytometry</subject><subject>Flow cytometry</subject><subject>HeLa Cells</subject><subject>heparin</subject><subject>HT29 Cells</subject><subject>Humans</subject><subject>MCF-7 Cells</subject><subject>Microscopy</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - pharmacokinetics</subject><subject>oligoproline</subject><subject>Peptides</subject><subject>Polysaccharides</subject><subject>Proline - analogs & derivatives</subject><subject>Proline - pharmacokinetics</subject><subject>Static Electricity</subject><subject>Tumor cell lines</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNqFkU1LAzEQhoMofl89yoIXL1uT7EeyR1mrFor2oOeQZidtynazJluknvwJ_kZ_iSmtFTwoc5hheOZh4EXojOAewZheycZAj2KSY5anxQ46JBklccJYshvmNElixjNygI68nwWec5zvowPKCow5zg6R7GsNqousjkYOrJsE4RtUUTmVbgKf7x83xre1XEa2ibopRCXUddiOoIHOyc40k3BnW3CdAb-ylGFpG6OiEbSdqcCfoD0taw-nm36Mnm_7T-V9PHy8G5TXw1hlOC3iirAExjqXmCQyk7rQFMOYsorginKtFCGp4oGQgBWFlBRaVRQYl5LLSmXJMbpce1tnXxbgOzE3XoV3ZQN24QXhaUbTIk_zgF78Qmd24ZrwnaCY5gUJxf-iCM8SynLKaaB6a0o5670DLVpn5tItBcFiFZFYRSS2EYWD8412MZ5DtcW_MwlAsQZeTQ3Lf3Ti-mHQ_5F_AeKFn3s</recordid><startdate>20170102</startdate><enddate>20170102</enddate><creator>Nagel, Yvonne A.</creator><creator>Raschle, Philipp S.</creator><creator>Wennemers, Helma</creator><general>Wiley Subscription Services, Inc</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>7TM</scope><scope>K9.</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3075-5741</orcidid></search><sort><creationdate>20170102</creationdate><title>Effect of Preorganized Charge‐Display on the Cell‐Penetrating Properties of Cationic Peptides</title><author>Nagel, Yvonne A. ; Raschle, Philipp S. ; Wennemers, Helma</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5049-d173ebf6a013a5af9f20eb27d10d28fcc114c8ebfae0c2e419fcd2e78aa8adc53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>Anticoagulants</topic><topic>arginine</topic><topic>Binding</topic><topic>Cancer</topic><topic>Cationic peptides</topic><topic>Cations</topic><topic>Cations - chemistry</topic><topic>Cations - pharmacokinetics</topic><topic>Cell Membrane Permeability</topic><topic>Cell surface</topic><topic>Cell-Penetrating Peptides - chemistry</topic><topic>Cell-Penetrating Peptides - pharmacokinetics</topic><topic>cellular uptake</topic><topic>CHO Cells</topic><topic>Confocal microscopy</topic><topic>Cricetulus</topic><topic>Cytometry</topic><topic>Flow cytometry</topic><topic>HeLa Cells</topic><topic>heparin</topic><topic>HT29 Cells</topic><topic>Humans</topic><topic>MCF-7 Cells</topic><topic>Microscopy</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - pharmacokinetics</topic><topic>oligoproline</topic><topic>Peptides</topic><topic>Polysaccharides</topic><topic>Proline - analogs & derivatives</topic><topic>Proline - pharmacokinetics</topic><topic>Static Electricity</topic><topic>Tumor cell lines</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nagel, Yvonne A.</creatorcontrib><creatorcontrib>Raschle, Philipp S.</creatorcontrib><creatorcontrib>Wennemers, Helma</creatorcontrib><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><jtitle>Angewandte Chemie International Edition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nagel, Yvonne A.</au><au>Raschle, Philipp S.</au><au>Wennemers, Helma</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of Preorganized Charge‐Display on the Cell‐Penetrating Properties of Cationic Peptides</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew Chem Int Ed Engl</addtitle><date>2017-01-02</date><risdate>2017</risdate><volume>56</volume><issue>1</issue><spage>122</spage><epage>126</epage><pages>122-126</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><coden>ACIEAY</coden><abstract>The effect of preorganized versus undefined charge display on the cellular uptake of cationic cell‐penetrating peptides (CPPs) was investigated by comparing conformationally well‐defined guanidinylated oligoprolines with flexible oligoarginines. Flow cytometry and confocal microscopy studies with different cancer cell lines (HeLa, MCF‐7, and HT‐29) showed that preorganization of cationic charges in lateral distances of ≈9 Å enhanced the cellular uptake of CPPs. Binding affinity measurements revealed tighter binding of analogues of cell‐surface glycans to the guanidinylated octaproline with localized charges compared to flexible octaarginine, a finding that was further correlated to the cellular uptake by studies with CHO cells deficient in glycans on the outer plasma membrane.
Matching charges: Cationic oligoprolines with charges at lateral distances of 9 Å penetrate into cancer cells at submicromolar concentrations. The cellular uptake correlates with binding affinity to the cell‐surface glycan analogue heparin with comparable distances between anionic sulfate moieties.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>27900805</pmid><doi>10.1002/anie.201607649</doi><tpages>5</tpages><edition>International ed. in English</edition><orcidid>https://orcid.org/0000-0002-3075-5741</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1433-7851 |
| ispartof | Angewandte Chemie International Edition, 2017-01, Vol.56 (1), p.122-126 |
| issn | 1433-7851 1521-3773 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1845249646 |
| source | Wiley |
| subjects | Animals Anticoagulants arginine Binding Cancer Cationic peptides Cations Cations - chemistry Cations - pharmacokinetics Cell Membrane Permeability Cell surface Cell-Penetrating Peptides - chemistry Cell-Penetrating Peptides - pharmacokinetics cellular uptake CHO Cells Confocal microscopy Cricetulus Cytometry Flow cytometry HeLa Cells heparin HT29 Cells Humans MCF-7 Cells Microscopy Oligopeptides - chemistry Oligopeptides - pharmacokinetics oligoproline Peptides Polysaccharides Proline - analogs & derivatives Proline - pharmacokinetics Static Electricity Tumor cell lines |
| title | Effect of Preorganized Charge‐Display on the Cell‐Penetrating Properties of Cationic Peptides |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T18%3A53%3A07IST&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=Effect%20of%20Preorganized%20Charge%E2%80%90Display%20on%20the%20Cell%E2%80%90Penetrating%20Properties%20of%20Cationic%20Peptides&rft.jtitle=Angewandte%20Chemie%20International%20Edition&rft.au=Nagel,%20Yvonne%20A.&rft.date=2017-01-02&rft.volume=56&rft.issue=1&rft.spage=122&rft.epage=126&rft.pages=122-126&rft.issn=1433-7851&rft.eissn=1521-3773&rft.coden=ACIEAY&rft_id=info:doi/10.1002/anie.201607649&rft_dat=%3Cproquest_cross%3E1845249646%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c5049-d173ebf6a013a5af9f20eb27d10d28fcc114c8ebfae0c2e419fcd2e78aa8adc53%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1853276282&rft_id=info:pmid/27900805&rfr_iscdi=true |