The Importance of Detail: How Differences in Ligand Structures Determine Distinct Functional Responses in Integrin αv β3.
Identifieur interne : 000223 ( Main/Exploration ); précédent : 000222; suivant : 000224The Importance of Detail: How Differences in Ligand Structures Determine Distinct Functional Responses in Integrin αv β3.
Auteurs : Antonella Paladino [Italie] ; Monica Civera [Italie] ; Flavio Curnis [Italie] ; Mayra Paolillo [Italie] ; Cesare Gennari [Italie] ; Umberto Piarulli [Italie] ; Angelo Corti [Italie] ; Laura Belvisi [Italie] ; Giorgio Colombo [Italie]Source :
- Chemistry (Weinheim an der Bergstrasse, Germany) [ 1521-3765 ] ; 2019.
Abstract
Ligand-based control of protein functional motions can provide novel opportunities in the study of fundamental biological mechanisms and in the development of novel therapeutics. In this work we addressed the ligand-based modulation of integrin functions. Inhibitors of integrin αv β3 are interesting anticancer agents but their molecular mechanisms are still unclear: Peptides and peptidomimetics characterized by the Arg-Gly-Asp (RGD) or isoAsp-Gly-Arg (isoDGR) binding motifs have shown controversial agonist/antagonist effects. We have investigated the differential mechanisms of integrin activation/deactivation by three distinct ligands (cyclo-RGDf(NMe)V (Cilengitide), cyclo[DKP3-RGD], cyclo[DKP3-isoDGR]; DKP=diketopiperazine) through a comparative analysis of ligand-controlled protein internal dynamics: Although RGD facilitates the onset of dynamic states leading to activation, isoDGR induces a diffuse rigidification of the complex consistent with antagonist activities. Computational predictions have been experimentally probed by showing that the antibody AP5, which is capable of recognizing the active form of integrin, binds specifically to the RGD complexes and not to the isoDGR complex, which supports opposite functional roles of the two motifs targeting the same binding site.
DOI: 10.1002/chem.201900169
PubMed: 30811704
Affiliations:
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α<sub>v</sub> β<sub>3</sub>.</title><author><name sortKey="Paladino, Antonella" sort="Paladino, Antonella" uniqKey="Paladino A" first="Antonella" last="Paladino">Antonella Paladino</name><affiliation wicri:level="3"><nlm:affiliation>Istituto di Chimica del Riconoscimento Molecolare CNR, via Mario Bianco 9, 20131, Milan, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Istituto di Chimica del Riconoscimento Molecolare CNR, via Mario Bianco 9, 20131, Milan</wicri:regionArea><placeName><settlement type="city">Milan</settlement><region nuts="2">Lombardie</region></placeName></affiliation></author><author><name sortKey="Civera, Monica" sort="Civera, Monica" uniqKey="Civera M" first="Monica" last="Civera">Monica Civera</name><affiliation wicri:level="3"><nlm:affiliation>Dipartimento di Chimica, Università degli Studi di Milano, via Golgi 19, 20133, Milan, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Chimica, 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uniqKey="Belvisi L" first="Laura" last="Belvisi">Laura Belvisi</name><affiliation wicri:level="3"><nlm:affiliation>Dipartimento di Chimica, Università degli Studi di Milano, via Golgi 19, 20133, Milan, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Chimica, Università degli Studi di Milano, via Golgi 19, 20133, Milan</wicri:regionArea><placeName><settlement type="city">Milan</settlement><region nuts="2">Lombardie</region></placeName></affiliation></author><author><name sortKey="Colombo, Giorgio" sort="Colombo, Giorgio" uniqKey="Colombo G" first="Giorgio" last="Colombo">Giorgio Colombo</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Chimica, Università degli Studi di Pavia, Viale Taramelli 12, 27100, Pavia, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Chimica, Università degli Studi di Pavia, Viale Taramelli 12, 27100, Pavia</wicri:regionArea><wicri:noRegion>Pavia</wicri:noRegion></affiliation></author></analytic><series><title level="j">Chemistry (Weinheim an der Bergstrasse, Germany)</title><idno type="eISSN">1521-3765</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ligand-based control of protein functional motions can provide novel opportunities in the study of fundamental biological mechanisms and in the development of novel therapeutics. In this work we addressed the ligand-based modulation of integrin functions. Inhibitors of integrin α<sub>v</sub> β<sub>3</sub> are interesting anticancer agents but their molecular mechanisms are still unclear: Peptides and peptidomimetics characterized by the Arg-Gly-Asp (RGD) or isoAsp-Gly-Arg (isoDGR) binding motifs have shown controversial agonist/antagonist effects. We have investigated the differential mechanisms of integrin activation/deactivation by three distinct ligands (cyclo-RGDf(NMe)V (Cilengitide), cyclo[DKP3-RGD], cyclo[DKP3-isoDGR]; DKP=diketopiperazine) through a comparative analysis of ligand-controlled protein internal dynamics: Although RGD facilitates the onset of dynamic states leading to activation, isoDGR induces a diffuse rigidification of the complex consistent with antagonist activities. Computational predictions have been experimentally probed by showing that the antibody AP5, which is capable of recognizing the active form of integrin, binds specifically to the RGD complexes and not to the isoDGR complex, which supports opposite functional roles of the two motifs targeting the same binding site.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">30811704</PMID><DateRevised><Year>2019</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1521-3765</ISSN><JournalIssue CitedMedium="Internet"><Volume>25</Volume><Issue>23</Issue><PubDate><Year>2019</Year><Month>Apr</Month><Day>23</Day></PubDate></JournalIssue><Title>Chemistry (Weinheim an der Bergstrasse, Germany)</Title><ISOAbbreviation>Chemistry</ISOAbbreviation></Journal><ArticleTitle>The Importance of Detail: How Differences in Ligand Structures Determine Distinct Functional Responses in Integrin α<sub>v</sub> β<sub>3</sub>.</ArticleTitle><Pagination><MedlinePgn>5959-5970</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/chem.201900169</ELocationID><Abstract><AbstractText>Ligand-based control of protein functional motions can provide novel opportunities in the study of fundamental biological mechanisms and in the development of novel therapeutics. In this work we addressed the ligand-based modulation of integrin functions. Inhibitors of integrin α<sub>v</sub> β<sub>3</sub> are interesting anticancer agents but their molecular mechanisms are still unclear: Peptides and peptidomimetics characterized by the Arg-Gly-Asp (RGD) or isoAsp-Gly-Arg (isoDGR) binding motifs have shown controversial agonist/antagonist effects. We have investigated the differential mechanisms of integrin activation/deactivation by three distinct ligands (cyclo-RGDf(NMe)V (Cilengitide), cyclo[DKP3-RGD], cyclo[DKP3-isoDGR]; DKP=diketopiperazine) through a comparative analysis of ligand-controlled protein internal dynamics: Although RGD facilitates the onset of dynamic states leading to activation, isoDGR induces a diffuse rigidification of the complex consistent with antagonist activities. Computational predictions have been experimentally probed by showing that the antibody AP5, which is capable of recognizing the active form of integrin, binds specifically to the RGD complexes and not to the isoDGR complex, which supports opposite functional roles of the two motifs targeting the same binding site.</AbstractText><CopyrightInformation>© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Paladino</LastName><ForeName>Antonella</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Istituto di Chimica del Riconoscimento Molecolare CNR, via Mario Bianco 9, 20131, Milan, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Civera</LastName><ForeName>Monica</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Dipartimento di Chimica, Università degli Studi di Milano, via Golgi 19, 20133, Milan, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Curnis</LastName><ForeName>Flavio</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>IRCCS Ospedale San Raffaele, Via Olgettina 60, 20132, Milan, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Paolillo</LastName><ForeName>Mayra</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Dipartimento di Scienze del Farmaco, Università degli Studi di Pavia, Viale Taramelli 6, 27100, Pavia, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gennari</LastName><ForeName>Cesare</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Dipartimento di Chimica, Università degli Studi di Milano, via Golgi 19, 20133, Milan, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Piarulli</LastName><ForeName>Umberto</ForeName><Initials>U</Initials><AffiliationInfo><Affiliation>Dipartimento di Scienza e Alta Tecnologia, Università degli Studi dell'Insubria, Via Valleggio 11, 22100, Como, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Corti</LastName><ForeName>Angelo</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>IRCCS Ospedale San Raffaele, Via Olgettina 60, 20132, Milan, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Belvisi</LastName><ForeName>Laura</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Dipartimento di Chimica, Università degli Studi di Milano, via Golgi 19, 20133, Milan, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Colombo</LastName><ForeName>Giorgio</ForeName><Initials>G</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-1318-668X</Identifier><AffiliationInfo><Affiliation>Dipartimento di Chimica, Università degli Studi di Pavia, Viale Taramelli 12, 27100, Pavia, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>IG 20019</GrantID><Agency>Associazione Italiana per la Ricerca sul Cancro</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>03</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Chemistry</MedlineTA><NlmUniqueID>9513783</NlmUniqueID><ISSNLinking>0947-6539</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">conformation analysis</Keyword><Keyword MajorTopicYN="N">flow cytometry analysis</Keyword><Keyword MajorTopicYN="N">molecular dynamics</Keyword><Keyword MajorTopicYN="N">peptidomimetics</Keyword><Keyword MajorTopicYN="N">proteins</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>01</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>02</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>2</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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