pubmed-article:15763255 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15763255 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
pubmed-article:15763255 | lifeskim:mentions | umls-concept:C0007577 | lld:lifeskim |
pubmed-article:15763255 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
pubmed-article:15763255 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:15763255 | pubmed:dateCreated | 2005-3-14 | lld:pubmed |
pubmed-article:15763255 | pubmed:abstractText | The functionalization of hydrogels for receptor-mediated cell adhesion is one approach for targeted cell and tissue engineering applications. In this study, polyacrylamide gel surfaces were functionalized with specific cell adhesion ligands via the self-assembly of a peptide-based heterodimer. The system was comprised of a cysteine-terminated monomer, A (MW approximately 5400), grafted to the polyacrylamide gels and a complementary ligand presenting monomer, B(X) (MW approximately 5800) that was designed to heterodimerize with A. Two ligand presenting monomers were synthesized: one presenting the RGDS ligand, B(D), for receptor-mediated cell adhesion, and the other, a control monomer presenting the nonadhesive RGES ligand, B(E). Assembly of the peptide pair A-B(X) by association of the monomers into a coiled coil was verified by circular dichroism in solution. Binding studies were conducted to determine the dissociation constant of the pair A-B(X), which was found to be K(D) approximately 10(-8) m. Polyacrylamide gels functionalized with A-B(X) heterodimers were evaluated for cell adhesion using bovine aortic endothelial cells (BAECs). Endothelial cells cultured on the A-B(D) functionalized surfaces demonstrated typical cell morphologies and expected spreading behavior as a function of the density of RGDS ligand, calculated as the amount of B(D) associated with grafted A on the surface of the gels. In contrast, A-B(E) linked surfaces supported no cell adhesion. The adhesion of the substrate was dynamically altered through the reassembly of A-B(X) dimers as B(D) molecules in the solution replaced B(E) molecules at the substrate. The molecular constructs described here demonstrate the potential to design a broad family of switchable peptides that impart the dynamic control of biofunctionality at an interface, which would be useful for precise manipulation of cell physiology. | lld:pubmed |
pubmed-article:15763255 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15763255 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15763255 | pubmed:language | eng | lld:pubmed |
pubmed-article:15763255 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15763255 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15763255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15763255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15763255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15763255 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15763255 | pubmed:month | Aug | lld:pubmed |
pubmed-article:15763255 | pubmed:issn | 0142-9612 | lld:pubmed |
pubmed-article:15763255 | pubmed:author | pubmed-author:DeGradoWillia... | lld:pubmed |
pubmed-article:15763255 | pubmed:author | pubmed-author:HammerDaniel... | lld:pubmed |
pubmed-article:15763255 | pubmed:author | pubmed-author:WillcoxP... | lld:pubmed |
pubmed-article:15763255 | pubmed:author | pubmed-author:LahrSteven... | lld:pubmed |
pubmed-article:15763255 | pubmed:author | pubmed-author:Reinhart-King... | lld:pubmed |
pubmed-article:15763255 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15763255 | pubmed:volume | 26 | lld:pubmed |
pubmed-article:15763255 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15763255 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15763255 | pubmed:pagination | 4757-66 | lld:pubmed |
pubmed-article:15763255 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:15763255 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:15763255 | pubmed:articleTitle | Dynamic heterodimer-functionalized surfaces for endothelial cell adhesion. | lld:pubmed |
pubmed-article:15763255 | pubmed:affiliation | Department of Bioengineering, University of Pennsylvania, 3320 Smith Walk, 120 Hayden Hall, Philadelphia, PA 19104, USA. | lld:pubmed |
pubmed-article:15763255 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15763255 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:15763255 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:15763255 | pubmed:publicationType | Evaluation Studies | lld:pubmed |
pubmed-article:15763255 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |