Identification of potential targets for an anticoagulant pectin.
Identifieur interne : 002074 ( Ncbi/Merge ); précédent : 002073; suivant : 002075Identification of potential targets for an anticoagulant pectin.
Auteurs : Aline Guimarães Santana [Brésil] ; Ana Helena Pereira Gracher [Brésil] ; André Luis Rüdiger [Brésil] ; Nilson Ivo Tonin Zanchin [Brésil] ; Paulo Costa Carvalho [Brésil] ; Thales Ricardo Cipriani [Brésil] ; Tatiana De Arruda Campos Brasil De Souza [Brésil]Source :
- Journal of proteomics [ 1876-7737 ] ; 2016.
Abstract
Heparin is a sulfated polysaccharide of animal origin showing excellent anticoagulant properties. Although it strongly inhibits the coagulation cascade, its interaction with multiple sites results in several side effects. An ideal alternative compound should not only possess anticoagulant and antithrombotic activities, but also provide specific binding to components of the coagulation cascade to decrease side effects and facilitate the control of pharmacologic actions in patient's body. In this work, we performed a scan of potential targets for chemically sulfated pectin from Citrus sinensis (SCP) that shows an efficient anticoagulant activity by combining proteomics and molecular docking techniques. Defining the interaction partners of SCP is fundamental to evaluate if its pharmacological side effects can be as harmful as those from heparin. SCP interacts directly with heparin cofactor II, probably favoring its interaction with thrombin. SCP interaction with antithrombin depends likely on its association with thrombin or factor Xa. In addition to the interaction with factors related to homeostasis, SCP may also act on the renin-angiotensin and on the complement systems.
DOI: 10.1016/j.jprot.2016.06.013
PubMed: 27318178
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Electronic address: tatianabrasil@fiocruz.br.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Instituto Carlos Chagas, FIOCRUZ/PR</wicri:regionArea><placeName><region type="state">Paraná (État)</region></placeName></affiliation></author></analytic><series><title level="j">Journal of proteomics</title><idno type="eISSN">1876-7737</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Heparin is a sulfated polysaccharide of animal origin showing excellent anticoagulant properties. Although it strongly inhibits the coagulation cascade, its interaction with multiple sites results in several side effects. An ideal alternative compound should not only possess anticoagulant and antithrombotic activities, but also provide specific binding to components of the coagulation cascade to decrease side effects and facilitate the control of pharmacologic actions in patient's body. In this work, we performed a scan of potential targets for chemically sulfated pectin from Citrus sinensis (SCP) that shows an efficient anticoagulant activity by combining proteomics and molecular docking techniques. Defining the interaction partners of SCP is fundamental to evaluate if its pharmacological side effects can be as harmful as those from heparin. SCP interacts directly with heparin cofactor II, probably favoring its interaction with thrombin. SCP interaction with antithrombin depends likely on its association with thrombin or factor Xa. In addition to the interaction with factors related to homeostasis, SCP may also act on the renin-angiotensin and on the complement systems.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">27318178</PMID><DateCreated><Year>2016</Year><Month>6</Month><Day>27</Day></DateCreated><DateRevised><Year>2016</Year><Month>6</Month><Day>27</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1876-7737</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2016</Year><Month>Jun</Month><Day>16</Day></PubDate></JournalIssue><Title>Journal of proteomics</Title><ISOAbbreviation>J Proteomics</ISOAbbreviation></Journal><ArticleTitle>Identification of potential targets for an anticoagulant pectin.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">S1874-3919(16)30252-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jprot.2016.06.013</ELocationID><Abstract><AbstractText NlmCategory="UNASSIGNED">Heparin is a sulfated polysaccharide of animal origin showing excellent anticoagulant properties. Although it strongly inhibits the coagulation cascade, its interaction with multiple sites results in several side effects. An ideal alternative compound should not only possess anticoagulant and antithrombotic activities, but also provide specific binding to components of the coagulation cascade to decrease side effects and facilitate the control of pharmacologic actions in patient's body. In this work, we performed a scan of potential targets for chemically sulfated pectin from Citrus sinensis (SCP) that shows an efficient anticoagulant activity by combining proteomics and molecular docking techniques. Defining the interaction partners of SCP is fundamental to evaluate if its pharmacological side effects can be as harmful as those from heparin. SCP interacts directly with heparin cofactor II, probably favoring its interaction with thrombin. SCP interaction with antithrombin depends likely on its association with thrombin or factor Xa. In addition to the interaction with factors related to homeostasis, SCP may also act on the renin-angiotensin and on the complement systems.</AbstractText><AbstractText Label="BIOLOGICAL SIGNIFICANCE" NlmCategory="UNASSIGNED">The knowledge of potential molecular targets of SCP provides clues to understand its mechanism of action in order to guide molecular changes in this compound to increase its specificity.</AbstractText><CopyrightInformation>Copyright © 2016 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Santana</LastName><ForeName>Aline Guimarães</ForeName><Initials>AG</Initials><AffiliationInfo><Affiliation>Instituto Carlos Chagas, FIOCRUZ/PR, Brazil; Universidade Federal do Paraná (UFPR), Departamento de Bioquímica e Biologia Molecular, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gracher</LastName><ForeName>Ana Helena Pereira</ForeName><Initials>AH</Initials><AffiliationInfo><Affiliation>Universidade Federal do Paraná (UFPR), Departamento de Bioquímica e Biologia Molecular, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rüdiger</LastName><ForeName>André Luis</ForeName><Initials>AL</Initials><AffiliationInfo><Affiliation>Universidade Federal do Paraná (UFPR), Departamento de Química, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zanchin</LastName><ForeName>Nilson Ivo Tonin</ForeName><Initials>NI</Initials><AffiliationInfo><Affiliation>Instituto Carlos Chagas, FIOCRUZ/PR, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carvalho</LastName><ForeName>Paulo Costa</ForeName><Initials>PC</Initials><AffiliationInfo><Affiliation>Instituto Carlos Chagas, FIOCRUZ/PR, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cipriani</LastName><ForeName>Thales Ricardo</ForeName><Initials>TR</Initials><AffiliationInfo><Affiliation>Universidade Federal do Paraná (UFPR), Departamento de Bioquímica e Biologia Molecular, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Arruda Campos Brasil de Souza</LastName><ForeName>Tatiana</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Instituto Carlos Chagas, FIOCRUZ/PR, Brazil. Electronic address: tatianabrasil@fiocruz.br.</Affiliation></AffiliationInfo></Author></AuthorList><Language>ENG</Language><PublicationTypeList><PublicationType UI="">JOURNAL ARTICLE</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>Jun</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Proteomics</MedlineTA><NlmUniqueID>101475056</NlmUniqueID><ISSNLinking>1874-3919</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Anticoagulant</Keyword><Keyword MajorTopicYN="N">Molecular targets</Keyword><Keyword MajorTopicYN="N">Sulfated pectin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>2</Month><Day>2</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>5</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>6</Month><Day>9</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>6</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>6</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>6</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27318178</ArticleId><ArticleId IdType="pii">S1874-3919(16)30252-4</ArticleId><ArticleId IdType="doi">10.1016/j.jprot.2016.06.013</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Brésil</li></country><region><li>Paraná (État)</li></region></list><tree><country name="Brésil"><noRegion><name sortKey="Santana, Aline Guimaraes" sort="Santana, Aline Guimaraes" uniqKey="Santana A" first="Aline Guimarães" last="Santana">Aline Guimarães Santana</name></noRegion><name sortKey="Carvalho, Paulo Costa" sort="Carvalho, Paulo Costa" uniqKey="Carvalho P" first="Paulo Costa" last="Carvalho">Paulo Costa Carvalho</name><name sortKey="Cipriani, Thales Ricardo" sort="Cipriani, Thales Ricardo" uniqKey="Cipriani T" first="Thales Ricardo" last="Cipriani">Thales Ricardo Cipriani</name><name sortKey="De Arruda Campos Brasil De Souza, Tatiana" sort="De Arruda Campos Brasil De Souza, Tatiana" uniqKey="De Arruda Campos Brasil De Souza T" first="Tatiana" last="De Arruda Campos Brasil De Souza">Tatiana De Arruda Campos Brasil De Souza</name><name sortKey="Gracher, Ana Helena Pereira" sort="Gracher, Ana Helena Pereira" uniqKey="Gracher A" first="Ana Helena Pereira" last="Gracher">Ana Helena Pereira Gracher</name><name sortKey="Rudiger, Andre Luis" sort="Rudiger, Andre Luis" uniqKey="Rudiger A" first="André Luis" last="Rüdiger">André Luis Rüdiger</name><name sortKey="Zanchin, Nilson Ivo Tonin" sort="Zanchin, Nilson Ivo Tonin" uniqKey="Zanchin N" first="Nilson Ivo Tonin" last="Zanchin">Nilson Ivo Tonin Zanchin</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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