PB28, the Sigma-1 and Sigma-2 Receptors Modulator With Potent Anti-SARS-CoV-2 Activity: A Review About Its Pharmacological Properties and Structure Affinity Relationships.
Identifieur interne : 000E88 ( Main/Exploration ); précédent : 000E87; suivant : 000E89PB28, the Sigma-1 and Sigma-2 Receptors Modulator With Potent Anti-SARS-CoV-2 Activity: A Review About Its Pharmacological Properties and Structure Affinity Relationships.
Auteurs : Carmen Abate [Italie] ; Mauro Niso [Italie] ; Francesca Serena Abatematteo [Italie] ; Marialessandra Contino [Italie] ; Nicola Antonio Colabufo [Italie] ; Francesco Berardi [Italie]Source :
- Frontiers in pharmacology [ 1663-9812 ] ; 2020.
Abstract
These unprecedented times have forced the scientific community to gather to face the COVID-19 pandemic. Efforts in diverse directions have been made. A multi-university team has focused on the identification of the host (human) proteins interacting with SARS-CoV-2 viral proteins, with the aim of hampering these interactions that may cause severe COVID-19 symptoms. Sigma-1 and sigma-2 receptors surprisingly belong to the "druggable" host proteins found, with the pan-sigma receptor modulator PB28 displaying the most potent anti-SARS-CoV-2 activity in in vitro assays. Being 20-fold more active than hydroxychloroquine, without cardiac side effects, PB28 is a promising antiviral candidate worthy of further investigation. Our research group developed PB28 in 1996 and have thoroughly characterized its biological properties since then. Structure-affinity relationship (SAfiR) studies at the sigma receptor subtypes were also undertaken with PB28 as the lead compound. We herein report our knowledge of PB28 to share information that may help to gain insight into the antiviral action of this compound and sigma receptors, while providing structural hints that may speed up the translation into therapeutics of this class of ligands.
DOI: 10.3389/fphar.2020.589810
PubMed: 33364961
PubMed Central: PMC7750835
Affiliations:
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Bari</wicri:regionArea><wicri:noRegion>Bari</wicri:noRegion></affiliation></author><author><name sortKey="Niso, Mauro" sort="Niso, Mauro" uniqKey="Niso M" first="Mauro" last="Niso">Mauro Niso</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Farmacia-Scienze del Farmaco, Università degli Studi di Bari ALDO MORO, Bari, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Farmacia-Scienze del Farmaco, Università degli Studi di Bari ALDO MORO, Bari</wicri:regionArea><wicri:noRegion>Bari</wicri:noRegion></affiliation></author><author><name sortKey="Abatematteo, Francesca Serena" sort="Abatematteo, Francesca Serena" uniqKey="Abatematteo F" first="Francesca Serena" last="Abatematteo">Francesca Serena Abatematteo</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Farmacia-Scienze del Farmaco, Università degli Studi di Bari ALDO MORO, Bari, Italy.</nlm:affiliation><country 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type="ISSN">1663-9812</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">These unprecedented times have forced the scientific community to gather to face the COVID-19 pandemic. Efforts in diverse directions have been made. A multi-university team has focused on the identification of the host (human) proteins interacting with SARS-CoV-2 viral proteins, with the aim of hampering these interactions that may cause severe COVID-19 symptoms. Sigma-1 and sigma-2 receptors surprisingly belong to the "druggable" host proteins found, with the pan-sigma receptor modulator PB28 displaying the most potent anti-SARS-CoV-2 activity in in vitro assays. Being 20-fold more active than hydroxychloroquine, without cardiac side effects, PB28 is a promising antiviral candidate worthy of further investigation. Our research group developed PB28 in 1996 and have thoroughly characterized its biological properties since then. Structure-affinity relationship (SAfiR) studies at the sigma receptor subtypes were also undertaken with PB28 as the lead compound. We herein report our knowledge of PB28 to share information that may help to gain insight into the antiviral action of this compound and sigma receptors, while providing structural hints that may speed up the translation into therapeutics of this class of ligands.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">33364961</PMID><DateRevised><Year>2020</Year><Month>12</Month><Day>31</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1663-9812</ISSN><JournalIssue CitedMedium="Print"><Volume>11</Volume><PubDate><Year>2020</Year></PubDate></JournalIssue><Title>Frontiers in pharmacology</Title><ISOAbbreviation>Front Pharmacol</ISOAbbreviation></Journal><ArticleTitle>PB28, the Sigma-1 and Sigma-2 Receptors Modulator With Potent Anti-SARS-CoV-2 Activity: A Review About Its Pharmacological Properties and Structure Affinity Relationships.</ArticleTitle><Pagination><MedlinePgn>589810</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fphar.2020.589810</ELocationID><Abstract><AbstractText>These unprecedented times have forced the scientific community to gather to face the COVID-19 pandemic. Efforts in diverse directions have been made. A multi-university team has focused on the identification of the host (human) proteins interacting with SARS-CoV-2 viral proteins, with the aim of hampering these interactions that may cause severe COVID-19 symptoms. Sigma-1 and sigma-2 receptors surprisingly belong to the "druggable" host proteins found, with the pan-sigma receptor modulator PB28 displaying the most potent anti-SARS-CoV-2 activity in in vitro assays. Being 20-fold more active than hydroxychloroquine, without cardiac side effects, PB28 is a promising antiviral candidate worthy of further investigation. Our research group developed PB28 in 1996 and have thoroughly characterized its biological properties since then. Structure-affinity relationship (SAfiR) studies at the sigma receptor subtypes were also undertaken with PB28 as the lead compound. We herein report our knowledge of PB28 to share information that may help to gain insight into the antiviral action of this compound and sigma receptors, while providing structural hints that may speed up the translation into therapeutics of this class of ligands.</AbstractText><CopyrightInformation>Copyright © 2020 Abate, Niso, Abatematteo, Contino, Colabufo and Berardi.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Abate</LastName><ForeName>Carmen</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Dipartimento di Farmacia-Scienze del Farmaco, Università degli Studi di Bari ALDO MORO, Bari, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Niso</LastName><ForeName>Mauro</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Dipartimento di Farmacia-Scienze del Farmaco, Università degli Studi di Bari ALDO MORO, Bari, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Abatematteo</LastName><ForeName>Francesca Serena</ForeName><Initials>FS</Initials><AffiliationInfo><Affiliation>Dipartimento di Farmacia-Scienze del Farmaco, Università degli Studi di Bari ALDO MORO, Bari, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Contino</LastName><ForeName>Marialessandra</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Dipartimento di Farmacia-Scienze del Farmaco, Università degli Studi di Bari ALDO MORO, Bari, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Colabufo</LastName><ForeName>Nicola Antonio</ForeName><Initials>NA</Initials><AffiliationInfo><Affiliation>Dipartimento di Farmacia-Scienze del Farmaco, Università degli Studi di Bari ALDO MORO, Bari, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Berardi</LastName><ForeName>Francesco</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Dipartimento di Farmacia-Scienze del Farmaco, Università degli Studi di Bari ALDO MORO, Bari, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>12</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Front Pharmacol</MedlineTA><NlmUniqueID>101548923</NlmUniqueID><ISSNLinking>1663-9812</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">PB28</Keyword><Keyword MajorTopicYN="N">SARS-CoV-2</Keyword><Keyword MajorTopicYN="N">sigma-1 receptor</Keyword><Keyword MajorTopicYN="N">sigma-2 receptor</Keyword><Keyword MajorTopicYN="N">structure-affinity relationships</Keyword></KeywordList><CoiStatement>The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>07</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>10</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>12</Month><Day>28</Day><Hour>12</Hour><Minute>5</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>12</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>12</Month><Day>29</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33364961</ArticleId><ArticleId IdType="doi">10.3389/fphar.2020.589810</ArticleId><ArticleId IdType="pii">589810</ArticleId><ArticleId 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Marialessandra" sort="Contino, Marialessandra" uniqKey="Contino M" first="Marialessandra" last="Contino">Marialessandra Contino</name><name sortKey="Niso, Mauro" sort="Niso, Mauro" uniqKey="Niso M" first="Mauro" last="Niso">Mauro Niso</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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