A Natural Bioactive Peptide from Pinctada fucata Pearls Can Be Used as a Potential Inhibitor of the Interaction between SARS-CoV-2 and ACE2 against COVID-19
The frequent occurrence of viral infections poses a serious threat to human life. Identifying effective antiviral components is urgent. In China, pearls have been important traditional medicinal ingredients since ancient times, exhibiting various therapeutic properties, including detoxification prop...
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| Veröffentlicht in: | International journal of molecular sciences 2024-07, Vol.25 (14), p.7902 |
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| container_title | International journal of molecular sciences |
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| creator | Wang, Yayu Wang, Qin Chen, Xinjiani Li, Bailei Zhang, Zhen Yao, Liping Liu, Xiaojun Zhang, Rongqing |
| description | The frequent occurrence of viral infections poses a serious threat to human life. Identifying effective antiviral components is urgent. In China, pearls have been important traditional medicinal ingredients since ancient times, exhibiting various therapeutic properties, including detoxification properties. In this study, a peptide, KKCH, which acts against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), was derived from
pearls. Molecular docking showed that it bound to the same pocket of the SARS-CoV-2 S protein and cell surface target angiotensin-converting enzyme II (ACE2). The function of KKCH was analyzed through surface plasmon resonance (SPR), Enzyme-Linked Immunosorbent Assays, immunofluorescence, and simulation methods using the SARS-CoV-2 pseudovirus and live virus. The results showed that KKCH had a good affinity for ACE2 (KD = 6.24 × 10
M) and could inhibit the binding of the S1 protein to ACE2 via competitive binding. As a natural peptide, KKCH inhibited the binding of the SARS-CoV-2 S1 protein to the surface of human BEAS-2B and HEK293T cells. Moreover, viral experiments confirmed the antiviral activity of KKCH against both the SARS-CoV-2 spike pseudovirus and SARS-CoV-2 live virus, with half-maximal inhibitory concentration (IC
) values of 398.1 μM and 462.4 μM, respectively. This study provides new insights and potential avenues for the prevention and treatment of SARS-CoV-2 infections. |
| doi_str_mv | 10.3390/ijms25147902 |
| format | Article |
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pearls. Molecular docking showed that it bound to the same pocket of the SARS-CoV-2 S protein and cell surface target angiotensin-converting enzyme II (ACE2). The function of KKCH was analyzed through surface plasmon resonance (SPR), Enzyme-Linked Immunosorbent Assays, immunofluorescence, and simulation methods using the SARS-CoV-2 pseudovirus and live virus. The results showed that KKCH had a good affinity for ACE2 (KD = 6.24 × 10
M) and could inhibit the binding of the S1 protein to ACE2 via competitive binding. As a natural peptide, KKCH inhibited the binding of the SARS-CoV-2 S1 protein to the surface of human BEAS-2B and HEK293T cells. Moreover, viral experiments confirmed the antiviral activity of KKCH against both the SARS-CoV-2 spike pseudovirus and SARS-CoV-2 live virus, with half-maximal inhibitory concentration (IC
) values of 398.1 μM and 462.4 μM, respectively. This study provides new insights and potential avenues for the prevention and treatment of SARS-CoV-2 infections.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms25147902</identifier><identifier>PMID: 39063143</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Angiotensin-Converting Enzyme 2 - chemistry ; Angiotensin-Converting Enzyme 2 - metabolism ; Animals ; Antiviral Agents - chemistry ; Antiviral Agents - pharmacology ; Antiviral drugs ; B cells ; Coronaviruses ; COVID-19 ; COVID-19 - virology ; COVID-19 Drug Treatment ; Disease transmission ; Health aspects ; HEK293 Cells ; Humans ; Hydrogen bonds ; Molecular Docking Simulation ; Pandemics ; Pearls ; Peptides ; Peptides - chemistry ; Peptides - pharmacology ; Pinctada ; Protein Binding ; Proteins ; SARS-CoV-2 - drug effects ; SARS-CoV-2 - metabolism ; Severe acute respiratory syndrome ; Severe acute respiratory syndrome coronavirus 2 ; Spike Glycoprotein, Coronavirus - chemistry ; Spike Glycoprotein, Coronavirus - metabolism</subject><ispartof>International journal of molecular sciences, 2024-07, Vol.25 (14), p.7902</ispartof><rights>COPYRIGHT 2024 MDPI AG</rights><rights>2024 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c311t-1c212bd38d2173f0b888d640f8f598efb2a04572a42bfe053f0e6188e742fef83</cites><orcidid>0000-0002-9033-4367</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27915,27916</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39063143$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Yayu</creatorcontrib><creatorcontrib>Wang, Qin</creatorcontrib><creatorcontrib>Chen, Xinjiani</creatorcontrib><creatorcontrib>Li, Bailei</creatorcontrib><creatorcontrib>Zhang, Zhen</creatorcontrib><creatorcontrib>Yao, Liping</creatorcontrib><creatorcontrib>Liu, Xiaojun</creatorcontrib><creatorcontrib>Zhang, Rongqing</creatorcontrib><title>A Natural Bioactive Peptide from Pinctada fucata Pearls Can Be Used as a Potential Inhibitor of the Interaction between SARS-CoV-2 and ACE2 against COVID-19</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>The frequent occurrence of viral infections poses a serious threat to human life. Identifying effective antiviral components is urgent. In China, pearls have been important traditional medicinal ingredients since ancient times, exhibiting various therapeutic properties, including detoxification properties. In this study, a peptide, KKCH, which acts against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), was derived from
pearls. Molecular docking showed that it bound to the same pocket of the SARS-CoV-2 S protein and cell surface target angiotensin-converting enzyme II (ACE2). The function of KKCH was analyzed through surface plasmon resonance (SPR), Enzyme-Linked Immunosorbent Assays, immunofluorescence, and simulation methods using the SARS-CoV-2 pseudovirus and live virus. The results showed that KKCH had a good affinity for ACE2 (KD = 6.24 × 10
M) and could inhibit the binding of the S1 protein to ACE2 via competitive binding. As a natural peptide, KKCH inhibited the binding of the SARS-CoV-2 S1 protein to the surface of human BEAS-2B and HEK293T cells. Moreover, viral experiments confirmed the antiviral activity of KKCH against both the SARS-CoV-2 spike pseudovirus and SARS-CoV-2 live virus, with half-maximal inhibitory concentration (IC
) values of 398.1 μM and 462.4 μM, respectively. This study provides new insights and potential avenues for the prevention and treatment of SARS-CoV-2 infections.</description><subject>Angiotensin-Converting Enzyme 2 - chemistry</subject><subject>Angiotensin-Converting Enzyme 2 - metabolism</subject><subject>Animals</subject><subject>Antiviral Agents - chemistry</subject><subject>Antiviral Agents - pharmacology</subject><subject>Antiviral drugs</subject><subject>B cells</subject><subject>Coronaviruses</subject><subject>COVID-19</subject><subject>COVID-19 - virology</subject><subject>COVID-19 Drug Treatment</subject><subject>Disease transmission</subject><subject>Health aspects</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Hydrogen bonds</subject><subject>Molecular Docking Simulation</subject><subject>Pandemics</subject><subject>Pearls</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>Pinctada</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>SARS-CoV-2 - drug effects</subject><subject>SARS-CoV-2 - metabolism</subject><subject>Severe acute respiratory syndrome</subject><subject>Severe acute respiratory syndrome coronavirus 2</subject><subject>Spike Glycoprotein, Coronavirus - chemistry</subject><subject>Spike Glycoprotein, Coronavirus - metabolism</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNptkktv1TAQhSMEoqWwY40ssWHRtH7k4SzTUMqVqraitNtoEo9bXyX2xXao-C_82PqqBQpCXnh0_M3RGXmy7C2jB0I09NCs58BLVtQN5c-yXVZwnlNa1c-f1DvZqxDWlHLBy-ZltpP6KsEKsZv9bMkZxMXDRI6MgzGa70gucBONQqK9m8mFsWMEBUQvI0RIj-CnQDqw5AjJVUBFIJCku4g2mmS0srdmMNF54jSJt5iEiH7r7SwZMN4hWnLZfrnMO3edcwJWkbY7TsUNGBsi6c6vVx9z1rzOXmiYAr55vPeyq0_HX7vP-en5yaprT_NRMBZzNnLGByWk4qwWmg5SSlUVVEtdNhL1wIEWZc2h4INGWiYEKyYl1gXXqKXYyz48-G68-7ZgiP1swojTBBbdEnpBZcmYZHWZ0Pf_oGu3eJvSbamiSYG4-EPdwIS9sdrFNP_WtG8lFXXFJWeJOvgPlY7C2YzOojZJ_6th_6Fh9C4Ej7rfeDOD_9Ez2m-XoX-6DAl_95h1GWZUv-Ffvy_uASlZq0w</recordid><startdate>20240719</startdate><enddate>20240719</enddate><creator>Wang, Yayu</creator><creator>Wang, Qin</creator><creator>Chen, Xinjiani</creator><creator>Li, Bailei</creator><creator>Zhang, Zhen</creator><creator>Yao, Liping</creator><creator>Liu, Xiaojun</creator><creator>Zhang, Rongqing</creator><general>MDPI AG</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>COVID</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-9033-4367</orcidid></search><sort><creationdate>20240719</creationdate><title>A Natural Bioactive Peptide from Pinctada fucata Pearls Can Be Used as a Potential Inhibitor of the Interaction between SARS-CoV-2 and ACE2 against COVID-19</title><author>Wang, Yayu ; 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Identifying effective antiviral components is urgent. In China, pearls have been important traditional medicinal ingredients since ancient times, exhibiting various therapeutic properties, including detoxification properties. In this study, a peptide, KKCH, which acts against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), was derived from
pearls. Molecular docking showed that it bound to the same pocket of the SARS-CoV-2 S protein and cell surface target angiotensin-converting enzyme II (ACE2). The function of KKCH was analyzed through surface plasmon resonance (SPR), Enzyme-Linked Immunosorbent Assays, immunofluorescence, and simulation methods using the SARS-CoV-2 pseudovirus and live virus. The results showed that KKCH had a good affinity for ACE2 (KD = 6.24 × 10
M) and could inhibit the binding of the S1 protein to ACE2 via competitive binding. As a natural peptide, KKCH inhibited the binding of the SARS-CoV-2 S1 protein to the surface of human BEAS-2B and HEK293T cells. Moreover, viral experiments confirmed the antiviral activity of KKCH against both the SARS-CoV-2 spike pseudovirus and SARS-CoV-2 live virus, with half-maximal inhibitory concentration (IC
) values of 398.1 μM and 462.4 μM, respectively. This study provides new insights and potential avenues for the prevention and treatment of SARS-CoV-2 infections.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>39063143</pmid><doi>10.3390/ijms25147902</doi><orcidid>https://orcid.org/0000-0002-9033-4367</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Angiotensin-Converting Enzyme 2 - chemistry Angiotensin-Converting Enzyme 2 - metabolism Animals Antiviral Agents - chemistry Antiviral Agents - pharmacology Antiviral drugs B cells Coronaviruses COVID-19 COVID-19 - virology COVID-19 Drug Treatment Disease transmission Health aspects HEK293 Cells Humans Hydrogen bonds Molecular Docking Simulation Pandemics Pearls Peptides Peptides - chemistry Peptides - pharmacology Pinctada Protein Binding Proteins SARS-CoV-2 - drug effects SARS-CoV-2 - metabolism Severe acute respiratory syndrome Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - chemistry Spike Glycoprotein, Coronavirus - metabolism |
| title | A Natural Bioactive Peptide from Pinctada fucata Pearls Can Be Used as a Potential Inhibitor of the Interaction between SARS-CoV-2 and ACE2 against COVID-19 |
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