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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure-activity relationship of human bone sialoprotein peptides</title><author><name sortKey="Rapuano, Bruce E" sort="Rapuano, Bruce E" uniqKey="Rapuano B" first="Bruce E." last="Rapuano">Bruce E. Rapuano</name><affiliation><nlm:aff id="A1"> Hospital for Special Surgery affiliated with the Weill Medical College of Cornell University, 535 East 70<sup>th</sup> Street, New York, NY 10021, USA</nlm:aff></affiliation></author><author><name sortKey="Macdonald, Daniel E" sort="Macdonald, Daniel E" uniqKey="Macdonald D" first="Daniel E." last="Macdonald">Daniel E. Macdonald</name><affiliation><nlm:aff id="A1"> Hospital for Special Surgery affiliated with the Weill Medical College of Cornell University, 535 East 70<sup>th</sup> Street, New York, NY 10021, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2"> James J. Peters VA Medical Center, 130 West Kingsbridge Road, Bronx, NY, 10468, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A3"> Langmuir Center for Colloids and Interfaces, Columbia University, 911 S.W. Mudd Building, Mail Code 4711, 500 West 120<sup>th</sup> Street, New York, NY 10027, USA</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24103036</idno><idno type="pmc">4102602</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4102602</idno><idno type="RBID">PMC:4102602</idno><idno type="doi">10.1111/eos.12081</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">000431</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000431</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structure-activity relationship of human bone sialoprotein peptides</title><author><name sortKey="Rapuano, Bruce E" sort="Rapuano, Bruce E" uniqKey="Rapuano B" first="Bruce E." last="Rapuano">Bruce E. Rapuano</name><affiliation><nlm:aff id="A1"> Hospital for Special Surgery affiliated with the Weill Medical College of Cornell University, 535 East 70<sup>th</sup> Street, New York, NY 10021, USA</nlm:aff></affiliation></author><author><name sortKey="Macdonald, Daniel E" sort="Macdonald, Daniel E" uniqKey="Macdonald D" first="Daniel E." last="Macdonald">Daniel E. Macdonald</name><affiliation><nlm:aff id="A1"> Hospital for Special Surgery affiliated with the Weill Medical College of Cornell University, 535 East 70<sup>th</sup> Street, New York, NY 10021, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2"> James J. Peters VA Medical Center, 130 West Kingsbridge Road, Bronx, NY, 10468, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A3"> Langmuir Center for Colloids and Interfaces, Columbia University, 911 S.W. Mudd Building, Mail Code 4711, 500 West 120<sup>th</sup> Street, New York, NY 10027, USA</nlm:aff></affiliation></author></analytic><series><title level="j">European journal of oral sciences</title><idno type="ISSN">0909-8836</idno><idno type="eISSN">1600-0722</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">In the current study, the relationship between the structure of the RGD-containing human bone sialoprotein (hBSP) peptide 278-293 and its attachment activity toward osteoblast-like (MC3T3) cells was investigated. This goal was accomplished by examining the comparative cell attachment activities of several truncated forms of peptide 278-293. Computer modeling of the various peptides was also performed to assess the role of secondary structure in peptide bioactivity. The elimination of the tyrosine-278 at the N-terminus resulted in a more dramatic loss of cell attachment activity compared to the removal of either tyrosine-293 or the arg-ala-tyr (291-293) tripeptide. Although the replacement of the RGD (arg-gly-asp) peptide moiety with peptide KAE (lys-ala-glu) resulted in a dramatic loss of cell attachment activity, a peptide containing RGE (arg-glyglu) in place of RGD retained 70-85 % of the parental peptide's attachment activity. These results suggest that the N-terminal RGD-flanking region of hBSP peptide 278-293, in particular the tyrosine-278 residue, represents a second cell attachment site that stabilizes the RGD-integrin receptor complex. Computer modeling also suggested that a β-turn encompassing RGD or RGE in some of the hBSP peptides may facilitate its binding to integrins by increasing the exposure of the tripeptide. This knowledge may be useful in the future design of biomimetic peptides which are more effective in promoting the attachment of osteogenic cells to implant surfaces in vivo.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">9504563</journal-id><journal-id journal-id-type="pubmed-jr-id">8729</journal-id><journal-id journal-id-type="nlm-ta">Eur J Oral Sci</journal-id><journal-id journal-id-type="iso-abbrev">Eur. J. Oral Sci.</journal-id><journal-title-group><journal-title>European journal of oral sciences</journal-title></journal-title-group><issn pub-type="ppub">0909-8836</issn><issn pub-type="epub">1600-0722</issn></journal-meta><article-meta><article-id pub-id-type="pmid">24103036</article-id><article-id pub-id-type="pmc">4102602</article-id><article-id pub-id-type="doi">10.1111/eos.12081</article-id><article-id pub-id-type="manuscript">NIHMS510452</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Structure-activity relationship of human bone sialoprotein peptides</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Rapuano</surname><given-names>Bruce E.</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>MacDonald</surname><given-names>Daniel E.</given-names></name><xref ref-type="aff" rid="A1">a</xref><xref ref-type="aff" rid="A2">b</xref><xref ref-type="aff" rid="A3">c</xref></contrib></contrib-group><aff id="A1"><label>a</label> Hospital for Special Surgery affiliated with the Weill Medical College of Cornell University, 535 East 70<sup>th</sup> Street, New York, NY 10021, USA</aff><aff id="A2"><label>b</label> James J. Peters VA Medical Center, 130 West Kingsbridge Road, Bronx, NY, 10468, USA</aff><aff id="A3"><label>c</label> Langmuir Center for Colloids and Interfaces, Columbia University, 911 S.W. Mudd Building, Mail Code 4711, 500 West 120<sup>th</sup> Street, New York, NY 10027, USA</aff><author-notes><corresp id="CR1">To whom reprint requests should be sent : Daniel E. MacDonald Hospital for Special Surgery 535 East 70<sup>th</sup> Street New York, NY 10021, USA. <email>dem14@columbia.edu</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>17</day><month>4</month><year>2014</year></pub-date><pub-date pub-type="epub"><day>17</day><month>9</month><year>2013</year></pub-date><pub-date pub-type="ppub"><month>12</month><year>2013</year></pub-date><pub-date pub-type="pmc-release"><day>01</day><month>12</month><year>2014</year></pub-date><volume>121</volume><issue>6</issue><fpage>600</fpage><lpage>609</lpage><pmc-comment>elocation-id from pubmed: 10.1111/eos.12081</pmc-comment>
<abstract><p id="P1">In the current study, the relationship between the structure of the RGD-containing human bone sialoprotein (hBSP) peptide 278-293 and its attachment activity toward osteoblast-like (MC3T3) cells was investigated. This goal was accomplished by examining the comparative cell attachment activities of several truncated forms of peptide 278-293. Computer modeling of the various peptides was also performed to assess the role of secondary structure in peptide bioactivity. The elimination of the tyrosine-278 at the N-terminus resulted in a more dramatic loss of cell attachment activity compared to the removal of either tyrosine-293 or the arg-ala-tyr (291-293) tripeptide. Although the replacement of the RGD (arg-gly-asp) peptide moiety with peptide KAE (lys-ala-glu) resulted in a dramatic loss of cell attachment activity, a peptide containing RGE (arg-glyglu) in place of RGD retained 70-85 % of the parental peptide's attachment activity. These results suggest that the N-terminal RGD-flanking region of hBSP peptide 278-293, in particular the tyrosine-278 residue, represents a second cell attachment site that stabilizes the RGD-integrin receptor complex. Computer modeling also suggested that a β-turn encompassing RGD or RGE in some of the hBSP peptides may facilitate its binding to integrins by increasing the exposure of the tripeptide. This knowledge may be useful in the future design of biomimetic peptides which are more effective in promoting the attachment of osteogenic cells to implant surfaces in vivo.</p></abstract><kwd-group><kwd>biomimetic</kwd><kwd>extracellular matrix</kwd><kwd>RGD peptide</kwd><kwd>integrins</kwd><kwd>osteoblasts</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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