The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor
The effect of the polyanionic polymer of inorganic polyphosphate (polyP) involved in innate immunity on the binding of the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein to the cellular ACE2 receptor was studied. The RBD surface comprises a basic amino acid stretch of four arginine re...
Gespeichert in:
| Veröffentlicht in: | Biomaterials science 2020-12, Vol.8 (23), p.663-661 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 661 |
|---|---|
| container_issue | 23 |
| container_start_page | 663 |
| container_title | Biomaterials science |
| container_volume | 8 |
| creator | Müller, Werner E. G Neufurth, Meik Schepler, Hadrian Wang, Shunfeng Tolba, Emad Schröder, Heinz C Wang, Xiaohong |
| description | The effect of the polyanionic polymer of inorganic polyphosphate (polyP) involved in innate immunity on the binding of the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein to the cellular ACE2 receptor was studied. The RBD surface comprises a basic amino acid stretch of four arginine residues which interact with the physiological polyP (polyP
40
) and polyP
3
. Subsequently, the interaction of RBD with ACE2 is sensitively inhibited. After the chemical modification of arginine, an increased inhibition by polyP, at a 1 : 1 molar ratio (polyP : RBP), is measured already at 0.1 μg mL
−1
. Heparin was ineffective. The results suggest a potential therapeutic benefit of polyP against SARS-CoV-2 infection.
The polymer polyphosphate, abundant in blood platelets, blocks the binding of the receptor-binding domain (RBD) of the SARS- spike (S)-protein to the angiotensin-converting enzyme 2 (ACE2) at low concentrations. |
| doi_str_mv | 10.1039/d0bm01244k |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmed_primary_33231598</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2463652984</sourcerecordid><originalsourceid>FETCH-LOGICAL-c429t-398f2f79854611879b731d5b1f70e89d24fcb9ae66c170285017be4ca2bbbc403</originalsourceid><addsrcrecordid>eNpd0U1LwzAYB_Agisr04l0JeBGhmrc2zXHO-YITwanX0qSp69Y2NUkP-_Zmm04wl4Q8vzz8yQPACUZXGFFxXSDZIEwYW-yAQ4IYj1jKxO72TNEBOHZujsLiXKAE74MDSgnFsUgPQf8201BWpsm9tlVew87Uy25mXDcLN1DWRi0cdN5UahaU9rZSwbdF1X5CU0Ifnk-Hr9NoZD4iAqdRZ43XVQu9WdeUruu-zi0cjsYEWq105409AntlXjt9_LMPwPvd-G30EE1e7h9Hw0mkGBE-oiItSclFGrME45QLySkuYolLjnQqCsJKJUWuk0RhjkgaI8ylZionUkrFEB2Ai03fkOqr185nTeVWkfJWm95lhCUMx5gkONDzf3RuetuGdCtFk5iIlAV1uVHKGuesLrPOVk1ulxlG2Woe2S26eV7P4yngs5-WvWx0saW_vx_A6QZYp7bVv4HSbw68jd4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2463652984</pqid></control><display><type>article</type><title>The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor</title><source>MEDLINE</source><source>Royal Society Of Chemistry Journals 2008-</source><creator>Müller, Werner E. G ; Neufurth, Meik ; Schepler, Hadrian ; Wang, Shunfeng ; Tolba, Emad ; Schröder, Heinz C ; Wang, Xiaohong</creator><creatorcontrib>Müller, Werner E. G ; Neufurth, Meik ; Schepler, Hadrian ; Wang, Shunfeng ; Tolba, Emad ; Schröder, Heinz C ; Wang, Xiaohong</creatorcontrib><description>The effect of the polyanionic polymer of inorganic polyphosphate (polyP) involved in innate immunity on the binding of the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein to the cellular ACE2 receptor was studied. The RBD surface comprises a basic amino acid stretch of four arginine residues which interact with the physiological polyP (polyP
40
) and polyP
3
. Subsequently, the interaction of RBD with ACE2 is sensitively inhibited. After the chemical modification of arginine, an increased inhibition by polyP, at a 1 : 1 molar ratio (polyP : RBP), is measured already at 0.1 μg mL
−1
. Heparin was ineffective. The results suggest a potential therapeutic benefit of polyP against SARS-CoV-2 infection.
The polymer polyphosphate, abundant in blood platelets, blocks the binding of the receptor-binding domain (RBD) of the SARS- spike (S)-protein to the angiotensin-converting enzyme 2 (ACE2) at low concentrations.</description><identifier>ISSN: 2047-4830</identifier><identifier>EISSN: 2047-4849</identifier><identifier>DOI: 10.1039/d0bm01244k</identifier><identifier>PMID: 33231598</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Angiotensin-Converting Enzyme 2 - chemistry ; Angiotensin-Converting Enzyme 2 - metabolism ; Antiviral Agents - chemistry ; Antiviral Agents - pharmacology ; Binding ; Binding Sites ; Biomedical materials ; Heparin ; Humans ; Molecular Docking Simulation ; Polymers - chemistry ; Polymers - pharmacology ; Polyphosphates - chemistry ; Polyphosphates - pharmacology ; Protein Binding - drug effects ; Proteins ; Receptors ; Severe acute respiratory syndrome coronavirus 2 ; Spike Glycoprotein, Coronavirus - chemistry ; Spike Glycoprotein, Coronavirus - metabolism</subject><ispartof>Biomaterials science, 2020-12, Vol.8 (23), p.663-661</ispartof><rights>Copyright Royal Society of Chemistry 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c429t-398f2f79854611879b731d5b1f70e89d24fcb9ae66c170285017be4ca2bbbc403</citedby><cites>FETCH-LOGICAL-c429t-398f2f79854611879b731d5b1f70e89d24fcb9ae66c170285017be4ca2bbbc403</cites><orcidid>0000-0002-3422-2344 ; 0000-0002-8223-3689 ; 0000-0003-1796-6314</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33231598$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Müller, Werner E. G</creatorcontrib><creatorcontrib>Neufurth, Meik</creatorcontrib><creatorcontrib>Schepler, Hadrian</creatorcontrib><creatorcontrib>Wang, Shunfeng</creatorcontrib><creatorcontrib>Tolba, Emad</creatorcontrib><creatorcontrib>Schröder, Heinz C</creatorcontrib><creatorcontrib>Wang, Xiaohong</creatorcontrib><title>The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor</title><title>Biomaterials science</title><addtitle>Biomater Sci</addtitle><description>The effect of the polyanionic polymer of inorganic polyphosphate (polyP) involved in innate immunity on the binding of the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein to the cellular ACE2 receptor was studied. The RBD surface comprises a basic amino acid stretch of four arginine residues which interact with the physiological polyP (polyP
40
) and polyP
3
. Subsequently, the interaction of RBD with ACE2 is sensitively inhibited. After the chemical modification of arginine, an increased inhibition by polyP, at a 1 : 1 molar ratio (polyP : RBP), is measured already at 0.1 μg mL
−1
. Heparin was ineffective. The results suggest a potential therapeutic benefit of polyP against SARS-CoV-2 infection.
The polymer polyphosphate, abundant in blood platelets, blocks the binding of the receptor-binding domain (RBD) of the SARS- spike (S)-protein to the angiotensin-converting enzyme 2 (ACE2) at low concentrations.</description><subject>Angiotensin-Converting Enzyme 2 - chemistry</subject><subject>Angiotensin-Converting Enzyme 2 - metabolism</subject><subject>Antiviral Agents - chemistry</subject><subject>Antiviral Agents - pharmacology</subject><subject>Binding</subject><subject>Binding Sites</subject><subject>Biomedical materials</subject><subject>Heparin</subject><subject>Humans</subject><subject>Molecular Docking Simulation</subject><subject>Polymers - chemistry</subject><subject>Polymers - pharmacology</subject><subject>Polyphosphates - chemistry</subject><subject>Polyphosphates - pharmacology</subject><subject>Protein Binding - drug effects</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Severe acute respiratory syndrome coronavirus 2</subject><subject>Spike Glycoprotein, Coronavirus - chemistry</subject><subject>Spike Glycoprotein, Coronavirus - metabolism</subject><issn>2047-4830</issn><issn>2047-4849</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpd0U1LwzAYB_Agisr04l0JeBGhmrc2zXHO-YITwanX0qSp69Y2NUkP-_Zmm04wl4Q8vzz8yQPACUZXGFFxXSDZIEwYW-yAQ4IYj1jKxO72TNEBOHZujsLiXKAE74MDSgnFsUgPQf8201BWpsm9tlVew87Uy25mXDcLN1DWRi0cdN5UahaU9rZSwbdF1X5CU0Ifnk-Hr9NoZD4iAqdRZ43XVQu9WdeUruu-zi0cjsYEWq105409AntlXjt9_LMPwPvd-G30EE1e7h9Hw0mkGBE-oiItSclFGrME45QLySkuYolLjnQqCsJKJUWuk0RhjkgaI8ylZionUkrFEB2Ai03fkOqr185nTeVWkfJWm95lhCUMx5gkONDzf3RuetuGdCtFk5iIlAV1uVHKGuesLrPOVk1ulxlG2Woe2S26eV7P4yngs5-WvWx0saW_vx_A6QZYp7bVv4HSbw68jd4</recordid><startdate>20201207</startdate><enddate>20201207</enddate><creator>Müller, Werner E. G</creator><creator>Neufurth, Meik</creator><creator>Schepler, Hadrian</creator><creator>Wang, Shunfeng</creator><creator>Tolba, Emad</creator><creator>Schröder, Heinz C</creator><creator>Wang, Xiaohong</creator><general>Royal Society of Chemistry</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>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3422-2344</orcidid><orcidid>https://orcid.org/0000-0002-8223-3689</orcidid><orcidid>https://orcid.org/0000-0003-1796-6314</orcidid></search><sort><creationdate>20201207</creationdate><title>The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor</title><author>Müller, Werner E. G ; Neufurth, Meik ; Schepler, Hadrian ; Wang, Shunfeng ; Tolba, Emad ; Schröder, Heinz C ; Wang, Xiaohong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c429t-398f2f79854611879b731d5b1f70e89d24fcb9ae66c170285017be4ca2bbbc403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Angiotensin-Converting Enzyme 2 - chemistry</topic><topic>Angiotensin-Converting Enzyme 2 - metabolism</topic><topic>Antiviral Agents - chemistry</topic><topic>Antiviral Agents - pharmacology</topic><topic>Binding</topic><topic>Binding Sites</topic><topic>Biomedical materials</topic><topic>Heparin</topic><topic>Humans</topic><topic>Molecular Docking Simulation</topic><topic>Polymers - chemistry</topic><topic>Polymers - pharmacology</topic><topic>Polyphosphates - chemistry</topic><topic>Polyphosphates - pharmacology</topic><topic>Protein Binding - drug effects</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Severe acute respiratory syndrome coronavirus 2</topic><topic>Spike Glycoprotein, Coronavirus - chemistry</topic><topic>Spike Glycoprotein, Coronavirus - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Müller, Werner E. G</creatorcontrib><creatorcontrib>Neufurth, Meik</creatorcontrib><creatorcontrib>Schepler, Hadrian</creatorcontrib><creatorcontrib>Wang, Shunfeng</creatorcontrib><creatorcontrib>Tolba, Emad</creatorcontrib><creatorcontrib>Schröder, Heinz C</creatorcontrib><creatorcontrib>Wang, Xiaohong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>MEDLINE - Academic</collection><jtitle>Biomaterials science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Müller, Werner E. G</au><au>Neufurth, Meik</au><au>Schepler, Hadrian</au><au>Wang, Shunfeng</au><au>Tolba, Emad</au><au>Schröder, Heinz C</au><au>Wang, Xiaohong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor</atitle><jtitle>Biomaterials science</jtitle><addtitle>Biomater Sci</addtitle><date>2020-12-07</date><risdate>2020</risdate><volume>8</volume><issue>23</issue><spage>663</spage><epage>661</epage><pages>663-661</pages><issn>2047-4830</issn><eissn>2047-4849</eissn><abstract>The effect of the polyanionic polymer of inorganic polyphosphate (polyP) involved in innate immunity on the binding of the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein to the cellular ACE2 receptor was studied. The RBD surface comprises a basic amino acid stretch of four arginine residues which interact with the physiological polyP (polyP
40
) and polyP
3
. Subsequently, the interaction of RBD with ACE2 is sensitively inhibited. After the chemical modification of arginine, an increased inhibition by polyP, at a 1 : 1 molar ratio (polyP : RBP), is measured already at 0.1 μg mL
−1
. Heparin was ineffective. The results suggest a potential therapeutic benefit of polyP against SARS-CoV-2 infection.
The polymer polyphosphate, abundant in blood platelets, blocks the binding of the receptor-binding domain (RBD) of the SARS- spike (S)-protein to the angiotensin-converting enzyme 2 (ACE2) at low concentrations.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>33231598</pmid><doi>10.1039/d0bm01244k</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-3422-2344</orcidid><orcidid>https://orcid.org/0000-0002-8223-3689</orcidid><orcidid>https://orcid.org/0000-0003-1796-6314</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2047-4830 |
| ispartof | Biomaterials science, 2020-12, Vol.8 (23), p.663-661 |
| issn | 2047-4830 2047-4849 |
| language | eng |
| recordid | cdi_pubmed_primary_33231598 |
| source | MEDLINE; Royal Society Of Chemistry Journals 2008- |
| subjects | Angiotensin-Converting Enzyme 2 - chemistry Angiotensin-Converting Enzyme 2 - metabolism Antiviral Agents - chemistry Antiviral Agents - pharmacology Binding Binding Sites Biomedical materials Heparin Humans Molecular Docking Simulation Polymers - chemistry Polymers - pharmacology Polyphosphates - chemistry Polyphosphates - pharmacology Protein Binding - drug effects Proteins Receptors Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - chemistry Spike Glycoprotein, Coronavirus - metabolism |
| title | The biomaterial polyphosphate blocks stoichiometric binding of the SARS-CoV-2 S-protein to the cellular ACE2 receptor |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-09T07%3A14%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20biomaterial%20polyphosphate%20blocks%20stoichiometric%20binding%20of%20the%20SARS-CoV-2%20S-protein%20to%20the%20cellular%20ACE2%20receptor&rft.jtitle=Biomaterials%20science&rft.au=M%C3%BCller,%20Werner%20E.%20G&rft.date=2020-12-07&rft.volume=8&rft.issue=23&rft.spage=663&rft.epage=661&rft.pages=663-661&rft.issn=2047-4830&rft.eissn=2047-4849&rft_id=info:doi/10.1039/d0bm01244k&rft_dat=%3Cproquest_pubme%3E2463652984%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2463652984&rft_id=info:pmid/33231598&rfr_iscdi=true |